ID A0A1C8XRI2_DUNSA Unreviewed; 506 AA. AC A0A1C8XRI2; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 02-OCT-2024, entry version 23. 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; core chlorophytes; Chlorophyceae; OC CS clade; 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 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|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|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 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|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|HAMAP-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 --------------------------------------------------------------------------- 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 AlphaFoldDB; A0A1C8XRI2; -. 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; 3. 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 {ECO:0000256|HAMAP-Rule:MF_00352}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00352}; KW Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171, ECO:0000256|HAMAP- KW Rule:MF_00352}; KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, 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|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00352}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00352}; Plastid {ECO:0000313|EMBL:AOH77102.1}. FT DOMAIN 64..484 FT /note="Nitrogenase/oxidoreductase component 1" FT /evidence="ECO:0000259|Pfam:PF00148" FT BINDING 64 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00352" FT BINDING 89 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00352" FT BINDING 149 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="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 //