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Database: UniProt
Entry: G8IWY8_9SPER
LinkDB: G8IWY8_9SPER
Original site: G8IWY8_9SPER 
ID   G8IWY8_9SPER            Unreviewed;       468 AA.
AC   G8IWY8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:0000313|EMBL:AET46709.1};
GN   ORFNames=PCL_10067 {ECO:0000313|EMBL:AET46709.1};
OS   Pinus pinceana.
OG   Plastid {ECO:0000313|EMBL:AET46709.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Strobus.
OX   NCBI_TaxID=71648 {ECO:0000313|EMBL:AET46709.1};
RN   [1] {ECO:0000313|EMBL:AET46709.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PINC13 {ECO:0000313|EMBL:AET46709.1};
RX   PubMed=22731878; DOI=10.1186/1471-2148-12-100;
RA   Parks M., Cronn R., Liston A.;
RT   "Separating the wheat from the chaff: mitigating the effects of noise in a
RT   plastome phylogenomic data set from Pinus L. (Pinaceae).";
RL   BMC Evol. Biol. 12:100-100(2012).
RN   [2] {ECO:0000313|EMBL:AXQ01998.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30091785; DOI=10.1002/ajb2.1139;
RA   Gernandt D.S., Resendiz Arias C., Terrazas T., Aguirre Dugua X.,
RA   Willyard A.;
RT   "Incorporating fossils into the Pinaceae tree of life.";
RL   Am. J. Bot. 105:1329-1344(2018).
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   -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000256|HAMAP-
CC       Rule:MF_00352}.
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DR   EMBL; JN854174; AET46709.1; -; Genomic_DNA.
DR   EMBL; MH612866; AXQ01998.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8IWY8; -.
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 {ECO:0000256|HAMAP-Rule:MF_00352};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Chlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Chloroplast {ECO:0000313|EMBL:AET46709.1};
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|HAMAP-Rule:MF_00352};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Plastid {ECO:0000313|EMBL:AET46709.1}.
FT   DOMAIN          22..436
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00352"
SQ   SEQUENCE   468 AA;  53269 MW;  16707D21D209DC08 CRC64;
     MSTKIDETIT FECETGNYHT FCPISCVSWL YQKIEDSFFL VVGTKTCGYF LQNALGVMIF
     AEPRYAMAEL EEGDISAHLN DYEELKTLCI RIRKDRDPSV IIWIGTCTTE IIKMDLEGMA
     PKLEYEIGVP ILVARANGLD YAFTQGEDTV LAVMAHRCPE QEFPIGESKE TKTKLFPFPL
     LKENKLVEYA NHPPLVIFGS LPSNLVSQLD TELRRQFIKV SGWLPAQRYA DLPSLGDGVY
     VCGVNPFLSR TATTLIRRKK CELIVAPFPI GPDGTRAWIE RICPVFGIEA QSLEEREERI
     WESLKDYLDL VRGKSVFFMG DNLLEISLAR FLIRCGMIVY EIGIPYMDKR YQAAELALLK
     DTCIRMCIPI PRIVEKPDNS NQIRRMRELQ PDLAITGMAH ANPLGARGIG TKWSVEFTFA
     QIHGFANARD VLELVTRPLR RNENLDNLDR TTLVRNKNEF YTSTPTPR
//
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