ID CHLN_PINCO Reviewed; 459 AA.
AC P26180;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 13-SEP-2023, entry version 84.
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}; Synonyms=gidA;
OS Pinus contorta (Shore pine) (Lodgepole pine).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3339;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=1912499; DOI=10.1007/bf00037061;
RA Lidholm J., Gustafsson P.;
RT "Homologues of the green algal gidA gene and the liverwort frxC gene are
RT present on the chloroplast genomes of conifers.";
RL Plant Mol. Biol. 17:787-798(1991).
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; X56200; CAA39660.1; -; Genomic_DNA.
DR PIR; S17742; S17742.
DR AlphaFoldDB; P26180; -.
DR SMR; P26180; -.
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; 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; ATP-binding; Chlorophyll biosynthesis; Chloroplast; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Plastid.
FT CHAIN 1..459
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000208618"
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 459 AA; 52122 MW; C9F28480286F81F0 CRC64;
MSTKIVETIT LECETGNYHS FCPISCVSWL YQKIEDSFFL VVGTKTCGYF LQNALGVMIF
AEPRYAMAEL EEGDISAHLN DYEELKTLCI RIRKDRDPSV IIWIGTCTTE IIKMDLEGMA
PKLEYEIGVP ILVARANGLD YAFTQGEDTV LAVMAHRCPD QEFPIGESKE TKKKLFPFPL
LKENNLVEYA NHPPLVIFGS LPSNLVSQLD TELRRQFIKV SGWLPAQRYA DLPSLGDGVY
VCGVNPFLSR TATTLIRRKK CELIVAPFPI GPDGTRAWIE RICPVFGIEA QSLEEIEERI
WESLKDYLDL VRGKSVFFMG DNLIEISIAR FLIRCGMIVY EIGIPYLDKR YQAAELALLK
KTCIRMCMPI PRIVEKPDNS NQIRRMRELK PDLAITGMAH ANPLGARGIG TKWSVEFTFA
QIHGFANARD VLELVTRPLR RNENLDNLDR TTLVRKNNK
//
