CHLN_NEPOL
ID CHLN_NEPOL Reviewed; 431 AA.
AC Q9T4F6;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 78.
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-1 {ECO:0000255|HAMAP-Rule:MF_00352};
GN and
GN Name=chlN-2 {ECO:0000255|HAMAP-Rule:MF_00352};
OS Nephroselmis olivacea (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX NCBI_TaxID=31312;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-484 / S-N-5-8;
RX PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA Turmel M., Otis C., Lemieux C.;
RT "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT olivacea: insights into the architecture of ancestral chloroplast
RT genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(1999).
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; AF137379; AAD54882.1; -; Genomic_DNA.
DR EMBL; AF137379; AAD54907.1; -; Genomic_DNA.
DR RefSeq; NP_050911.1; NC_000927.1.
DR RefSeq; NP_050936.1; NC_000927.1.
DR AlphaFoldDB; Q9T4F6; -.
DR SMR; Q9T4F6; -.
DR GeneID; 801993; -.
DR GeneID; 801995; -.
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..431
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000208616"
FT BINDING 29
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 54
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 114
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 431 AA; 48314 MW; 3F21AD3276BBA69D CRC64;
MLSDQVTTAE LHPSAPLTEC ETGIYHTFCP ISCVAWLYQR VEDSFFLVIG TKTCGYFLQN
ALGVMIFAEP RYAMAELEEG DISAQFNDYH ELRRLCVQIQ QDRHPSVIVW IGTCTTEIIK
MDLEGMAPTL QAEIGIPIVV ARANGLDYAF TQGEDTVLAA MAQRCPDWTP DRTATQSTSS
PPLVIFGSVP ATVVSQLTFE LQRQKVEVTG WLPSARYADL PAVGEDVYAC GVNPFLSRTA
ITLMRRRRCK MIGSPFPIGP DGTRAWIEKI CHVFGLETTG LAERERQVWS QLEDYLSLVR
GKSAFLMGDN LLEISLARFL IRCGMIVHEV GIPYMDARFQ AAELHLLMRT CEAAHVPMPR
IVTKPDNFYQ VQRMRDVQPD LAITGMAHAN PLEARGTGTK WSVELTFWQL HGFASAKDLL
ELVTRPLRRT H
