ID   CHLN_SYNY3              Reviewed;         469 AA.
AC   P28372;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-SEP-2026, entry version 142.
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=slr0750;
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1368342; DOI=10.1271/bbb.56.788;
RA   Ogura Y., Takemura M., Oda K., Yamato K., Ohta E., Fukuzawa H., Ohyama K.;
RT   "Cloning and nucleotide sequence of a frxC-ORF469 gene cluster of
RT   Synechocystis PCC6803: conservation with liverwort chloroplast frxC-ORF465
RT   and nif operon.";
RL   Biosci. Biotechnol. Biochem. 56:788-793(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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=chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2
CC         phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] +
CC         2 ATP + 2 H2O; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002, Rhea:RHEA-
CC         COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33722,
CC         ChEBI:CHEBI:33723, ChEBI:CHEBI:43474, ChEBI:CHEBI:83348,
CC         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}.
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DR   EMBL; D10474; BAA01276.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18746.1; -; Genomic_DNA.
DR   PIR; JT0601; JT0601.
DR   AlphaFoldDB; P28372; -.
DR   SMR; P28372; -.
DR   IntAct; P28372; 2.
DR   STRING; 1148.gene:10500518; -.
DR   PaxDb; 1148-gene:10500518; -.
DR   EnsemblBacteria; BAA18746; BAA18746; BAA18746.
DR   KEGG; syn:slr0750; -.
DR   eggNOG; COG2710; Bacteria.
DR   InParanoid; P28372; -.
DR   PhylomeDB; P28372; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000001425; 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: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-UniRule.
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   NCBIfam; NF002768; PRK02842.1; 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; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding; Oxidoreductase; Photosynthesis;
KW   Reference proteome.
FT   CHAIN           1..469
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit N"
FT                   /id="PRO_0000208605"
FT   BINDING         24
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         49
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         109
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   469 AA;  52475 MW;  0A1BC3A7C4BBD84A CRC64;
     MTVAQQAPSA LNFDCETGNY HTFCPISCVS WLYQKIEDSF FLVIGTKTCG YFLQNAMGVM
     IFAEPRYAMA ELEEGDISAQ LKDYEELKRL CLQIKRDRNP SVIVWIGTCT TEIIKMDLEG
     LAPQLEAEIG IPIVTARANG LDYAFTQGED TVLASMAHKC PTSAQVQGED KEERNAIQKL
     LTFGRKADQE KVESEYVDHQ PLVLFGSLPD PVVTNLTLEL KKQGVKVSGW LPAKRYTELP
     VIDEGYYVAG VNPFLSRTAT TLMRRRKCKL IGAPFPIGPD GTRAWIEKIC SVLGIEPQGL
     EEREAQIWAS LEDYIQLIRG KSVFFMGDNL LEVSLARFLI RCGMTCPEIG IPYMDKRYQA
     AELALLEKTC SDMGVPLPNI VEKPDNYNQI QRIKALQPDL VITGMAHANP LEAQGINTKW
     SVEFTFAQIH GFTNARDILE LATRPLRRNS QLGELGWDKL IAKDVPAQV
//