ID CHLN_PROMA Reviewed; 418 AA. AC Q7VD37; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 95. 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}; GN OrderedLocusNames=Pro_0546; OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=167539; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SARG / CCMP1375 / SS120; RX PubMed=12917486; DOI=10.1073/pnas.1733211100; RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.; RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a RT nearly minimal oxyphototrophic genome."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003). 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 -!- 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; AE017126; AAP99591.1; -; Genomic_DNA. DR RefSeq; NP_874939.1; NC_005042.1. DR RefSeq; WP_011124700.1; NC_005042.1. DR PDB; 2YNM; X-ray; 2.10 A; C=1-418. DR PDBsum; 2YNM; -. DR AlphaFoldDB; Q7VD37; -. DR SMR; Q7VD37; -. DR IntAct; Q7VD37; 1. DR STRING; 167539.Pro_0546; -. DR EnsemblBacteria; AAP99591; AAP99591; Pro_0546. DR KEGG; pma:Pro_0546; -. DR PATRIC; fig|167539.5.peg.561; -. DR eggNOG; COG2710; Bacteria. DR HOGENOM; CLU_037170_0_0_3; -. DR OrthoDB; 5714774at2; -. DR UniPathway; UPA00670; -. DR Proteomes; UP000001420; Chromosome. 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 Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3. DR HAMAP; MF_00352; ChlN_BchN; 1. 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 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Iron; KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase; KW Photosynthesis; Reference proteome. FT CHAIN 1..418 FT /note="Light-independent protochlorophyllide reductase FT subunit N" FT /id="PRO_0000324008" FT BINDING 17 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 42 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 103 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 STRAND 4..9 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 22..28 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 32..38 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 40..50 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 76..90 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 95..101 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 103..107 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 112..123 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:2YNM" FT TURN 136..138 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 143..152 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 163..168 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 172..184 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 218..226 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 239..253 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 258..283 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 287..290 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 297..306 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 311..318 FT /evidence="ECO:0007829|PDB:2YNM" FT TURN 322..324 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 326..331 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 337..341 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 344..354 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 357..361 FT /evidence="ECO:0007829|PDB:2YNM" FT TURN 363..365 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 366..371 FT /evidence="ECO:0007829|PDB:2YNM" FT STRAND 376..378 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 379..384 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:2YNM" FT HELIX 393..410 FT /evidence="ECO:0007829|PDB:2YNM" SQ SEQUENCE 418 AA; 46199 MW; 02458DD9AD581EE5 CRC64; MSGSTLLKET GPREVFCGLT SIVWLHRRMP DAFFLVVGSR TCAHLIQSAA GVMIFAEPRF GTAILEERDL AGLADAHEEL DRVVKSLLKR RPEIRTLFLV GSCPSEVIKI DLSRAAERLS SQFNGQVRIL NYSGSGIETT FTQGEDGALK ALVPLMPSSQ EEQLLLAGTL ANPVEDRLKT IFNRLGIQKV ESFPPRESTK LPAIGPGTKV LLAQPYLTDT ARELKDRGAE ILQAPFPLGV EGSQLWIEAA ANAFKIKKTL VDATLEPLIT RAHKALKPYV EQLSGKKLFL LPESQLEIPL ARFLSNECGM KLIEVGVPYL NREMMGPELD LLPQNTRIVE GQHVEKQLDR VREHHPDLVV CGMGLANPLE AEGISTKWSI EMVFSPIHGI DQASDLAELF ARPLHRQNLL NKKTLEAV //