CHLN_ANTAG
ID CHLN_ANTAG Reviewed; 471 AA.
AC Q85A72;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
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 Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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 -!- RNA EDITING: Modified_positions=30 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 32 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 60 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 65 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 70 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 85 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 101 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 111 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 143 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 145 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 151 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 152 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 254 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 255 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 256 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 258 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 277 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 325 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 326 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 353 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 364 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 366 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 379 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 429 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 440 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions 32,
CC 145, 254 and 429 are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|HAMAP-
CC Rule:MF_00352}.
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DR EMBL; AB086179; BAC55410.1; -; Genomic_DNA.
DR EMBL; AB087493; BAC55510.1; -; mRNA.
DR RefSeq; NP_777473.1; NC_004543.1.
DR AlphaFoldDB; Q85A72; -.
DR SMR; Q85A72; -.
DR GeneID; 2553489; -.
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 2: Evidence at transcript level;
KW 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Chloroplast; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Plastid; RNA editing.
FT CHAIN 1..471
FT /note="Light-independent protochlorophyllide reductase
FT subunit N"
FT /id="PRO_0000208607"
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 471 AA; 53611 MW; E0A6A6B9621CDE73 CRC64;
MSIQISETLT FECETGNYHT FCPISCVAWL YQKIEDSFFL VIGTKTCGYF LQNALGVMIF
AEPRYAMAEL EEGDISAQLN DYEELKRLCF QIKKDRNPSV IIWIGTCTTE IIKMDLEGMA
PKLEVELGVP IVVARANGLD YAFTQGEDTV LAAMAHRCPE RDLLIDENKV IQNQTIQNIF
SLFSQKKKEE TLKYLELKNH PPLVLFGSLP STVASQLSLE LKRQSIQVSG WLPTQRYTDL
PSLGDGVYVC GVNPFLSRTA TTLIRRRKCK LIGAPFPIGP DGTRAWIEKI SSVFGIKTKG
LEEREQQVWQ SLKNYLNLVR GKSVFFMGDN LLEISLARFL IRCGMIVYEI GIPYMDKRYQ
AAELALLRNT CREMCTPMPR IVEKPDNYNQ IQRMRELQPD LAITGMAHAN PLEARGINTK
WSVEFTFAQI HGFTNAKDVL ELVTRPLRRN NSLEDLGWTN LIKKDNKIKV I
