ID   CHLN_NEOYE              Reviewed;         441 AA.
AC   Q1XDU9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 54.
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   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) 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: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}.
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DR   EMBL; AP006715; BAE92312.1; -; Genomic_DNA.
DR   RefSeq; YP_536869.1; NC_007932.1.
DR   AlphaFoldDB; Q1XDU9; -.
DR   SMR; Q1XDU9; -.
DR   GeneID; 3978845; -.
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   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; ATP-binding; Chlorophyll biosynthesis; Chloroplast; Iron;
KW   Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW   Photosynthesis; Plastid.
FT   CHAIN           1..441
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit N"
FT                   /id="PRO_0000275272"
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   441 AA;  49692 MW;  FF7CF7F474AC61FA CRC64;
     MSTAQSDALT FECETGNYHT FCPISCVSWL YQKIEDSFFL VIGTKTCGYF LQNAMGVMIF
     AEPRYAMAEL EEGDISAKLN DYGELRRLCL QIKKDRNPSV IFWIGTCTTE IIKMDLEGIA
     PKLEAEIRVP IVVARANGLD YAFTQGEDTV LAAMAQRCPL NLKNQSDNTS LKTSPHIPLV
     LFGSLPDPVV TQLTMELKKQ GIFVSGWLPS KRYTELPVIK EGYYVAGVNP FLSRTATTLM
     RRRKTKLIGA PFPIGPDGTR AWIEKICSVM NVKPIGLEDR EKAIWASLED YISLIRGKSV
     FFMGDNLLEV SLARFLTRCG MTVYEIGIPY MDKRYQAAEL ALLKATCDKM NVMMPTIVEK
     PDNYNQVDRI RDLKPDLVIT GMAHANPLEA RGINTKWSVE FTFAQIHGFT NARDILELVT
     RPLRRNLSLS ELGWDVYSKQ S