AC MF_00352; DC Protein; auto TR HAMAP; MF_00352; -; 1; level=0 XX Names: ChlN_BchN XX case and not ID BCHN end case case or ID CHLN end case DE RecName: Full=Light-independent protochlorophyllide reductase subunit N; DE Short=DPOR subunit N; DE Short=LI-POR subunit N; DE EC=1.3.7.7; case and not GN Name=bchN; end case case or GN Name=chlN; end case XX case and not 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 (BchN-BchB) is the CC catalytic component of the complex. CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll CC biosynthesis (light-independent). CC -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits; CC BchL, BchN and BchB. Forms a heterotetramer of two BchB and two BchN CC subunits. end case case or 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. CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll CC biosynthesis (light-independent). 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. end case 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; case CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at CC the heterodimer interface by residues from both subunits.; end case case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case CC -!- SIMILARITY: Belongs to the BchN/ChlN family. XX DR Pfam; PF00148; Oxidored_nitro; 1; trigger=no DR PIRSF; PIRSF000162; P_chlorophyll_rd; 1; trigger=no DR NCBIfam; TIGR01279; DPOR_bchN; 1; trigger=no XX KW ATP-binding KW Chlorophyll biosynthesis case and not KW Bacteriochlorophyll biosynthesis end case case KW 4Fe-4S KW Iron KW Iron-sulfur KW Metal-binding end case KW Nucleotide-binding KW Oxidoreductase KW Photosynthesis XX GO GO:0005524; F:ATP binding GO GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor case GO GO:0051539; F:4 iron, 4 sulfur cluster binding end case case and not GO GO:0030494; P:bacteriochlorophyll biosynthetic process end case case or GO GO:0015995; P:chlorophyll biosynthetic process end case GO GO:0015979; P:photosynthesis case GO GO:0009507; C:chloroplast end case XX FT From: BCHN_RHOCB (P26164) FT BINDING 26 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric FT partner" FT Group: 1; Condition: C FT BINDING 51 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric FT partner" FT Group: 1; Condition: C FT BINDING 112 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric FT partner" FT Group: 1; Condition: C XX Size: 410-500; Related: None; Template: P26164; Scope: Bacteria Plastid Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Divergent CHLRE, OLTVI, SCEOB not shown in alignment and not used in size range. External expert: Yuichi Fujita, fujita@protein.osaka-u.ac.jp XX # Revision 1.45 2023/06/01 //