ID G8J4C9_PINDE Unreviewed; 467 AA.
AC G8J4C9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:0000256|HAMAP-Rule:MF_00352,
GN ECO:0000313|EMBL:AET49300.1};
GN ORFNames=PCL_3067 {ECO:0000313|EMBL:AET49300.1};
OS Pinus densiflora (Japanese red pine).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AET49300.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=77912 {ECO:0000313|EMBL:AET49300.1};
RN [1] {ECO:0000313|EMBL:AET49300.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DENS02 {ECO:0000313|EMBL:AET49300.1};
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:AZA06105.1}
RP NUCLEOTIDE SEQUENCE.
RA Kim S.-C., Lee J.-W., Baek S.-H., Ahn J.-Y., Hong K.-N.;
RT "Identification of DNA molecular markers by comparison of Pinus densiflora
RT and Pinus sylvestris chloroplast genomes.";
RL PeerJ 0:0-0(2018).
RN [3] {ECO:0000313|EMBL:QBZ38280.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=333-360 {ECO:0000313|EMBL:QBZ38280.1};
RA Shim D., Kang H.-I., Lee H.O., Park T.S., Kim I.S., Lee S.W.;
RT "Complete Chloroplast Genome of Korean Red Pine (Pinus densiflora) using
RT Oxford Nanopore Technology and Illumina MiSeq.";
RL Submitted (DEC-2018) 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:0000256|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: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 -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis (light-independent). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00352}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_00352}.
CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000256|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; JN854210; AET49300.1; -; Genomic_DNA.
DR EMBL; MF990371; AZA06105.1; -; Genomic_DNA.
DR EMBL; MK285358; QBZ38280.1; -; Genomic_DNA.
DR AlphaFoldDB; G8J4C9; -.
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|ARBA:ARBA00023171, ECO:0000256|HAMAP-
KW Rule:MF_00352}; Chloroplast {ECO:0000313|EMBL:AET49300.1};
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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00352};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_00352}; Plastid {ECO:0000313|EMBL:AET49300.1}.
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 467 AA; 53047 MW; BD234A4A0C395F2D CRC64;
MSTKIVETIT LECETGNYHS FCPISCVSWL YQKIEDSFFL VVGTKTCGYF LQNALGVMIF
AEPRYAMAEL EEGDISAHLN DYEELKTLCI RIRKDRDPSV IIWIGTCTTE IIKMDLEGMA
PKLEYEIGVP ILVARANGLD YAFTQGEDTV LAVMAHRCPD QEFPIGESKE TKTKLFPFPL
LKEKNLVEYA NHPPLVIFGS LPSNLVSQLD TELRRQFIKV SGWLPAQRYA DLPSLGDGVY
VCGVNPFLSR TATTLIRRKK CELIVAPFPI GPDGTRAWIE RICPVFGIEA QSLEEREERI
WESLKDYLDL VRGKSVFFMG DNLIEISIAR FLIRCGMIVY EIGIPYMDKR YQAAELALLQ
NTCIRMCMPI PRIVEKPDNS NQIRRMRELQ PDLAITGMAH ANPLGARGIG TKWSVEFTFA
QIHGFANARD VLELVTRPLR RNENLDNLDR TTLVRKNNEL YTSTPVK
//
