CHLN_CHLRE
ID CHLN_CHLRE Reviewed; 545 AA.
AC P29683; B7U1J6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1374710; DOI=10.1002/j.1460-2075.1992.tb05220.x;
RA Choquet Y., Rahire M., Girard-Bascou J., Erickson J., Rochaix J.-D.;
RT "A chloroplast gene is required for the light-independent accumulation of
RT chlorophyll in Chlamydomonas reinhardtii.";
RL EMBO J. 11:1697-1704(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [3]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACJ50143.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY160685; AAN41268.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50143.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK000554; DAA00956.1; -; Genomic_DNA.
DR PIR; S20968; S20968.
DR RefSeq; NP_958412.2; NC_005353.1.
DR AlphaFoldDB; P29683; -.
DR SMR; P29683; -.
DR STRING; 3055.DAA00956; -.
DR PaxDb; P29683; -.
DR PRIDE; P29683; -.
DR GeneID; 2716986; -.
DR KEGG; cre:ChreCp056; -.
DR eggNOG; ENOG502QQ7U; Eukaryota.
DR HOGENOM; CLU_037170_0_0_1; -.
DR InParanoid; P29683; -.
DR OrthoDB; 725333at2759; -.
DR BioCyc; MetaCyc:MON-17821; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000006906; Chloroplast.
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 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; Reference proteome.
FT CHAIN 1..545
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000208610"
FT BINDING 102
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 127
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 187
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 VARIANT 476
FT /note="R -> Q (in strain: CC-503)"
FT VARIANT 529
FT /note="Q -> R (in strain: CC-503)"
SQ SEQUENCE 545 AA; 60868 MW; 1DD1660CD4D47EB1 CRC64;
MKPLKLKRLI MENNKSHATN LSLGGPFQGN CMPINQYFSK NQPNRGSSSS EKRSSLLPLW
ESKNAADGFS IVSHNVLLDG ATTILNLNSF FECETGNYHT FCPISCVAWL YQKIEDSFFL
VIGTKTCGYF LQNALGVMIF AEPRYAMAEL EESDISAQLN DYKELKRLCL QIKQDRNPSV
IVWIGTCTTE IIKMDLEGMA PRLETEIGIP IVVARANGLD YAFTQGEDTV LSAMALASLK
KDVPFLVGNT GLTNNQLLLE KSTSSVNGTD GKELLKKSLV LFGSVPSTVT TQLTLELKKE
GINVSGWLPS ANYKDLPTFN KDTLVCGINP FLSRTATTLM RRSKCTLICA PFPIGPDGTR
VWIEKICGAF GINPSLNPIT GNTNLYDREQ KIFNGLEDYL KLLRGKSVFF MGDNLLEISL
ARFLTRCGMI VYEIGIPYLD KRFQAAELAL LEQTCKEMNV PMPRIVEKPD NYYQIRRIRE
LKPDLTITGM AHANPLEARG ITTKWSVEFT FAQIHGFTNT REILELVTQP LRRNLMSNQS
VNAIS
