ID BCHN_RHOCB Reviewed; 424 AA. AC P26164; D5ANS6; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 04-NOV-2026, entry version 126. 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, ECO:0000269|PubMed:18358835}; GN Name=bchN {ECO:0000255|HAMAP-Rule:MF_00352}; GN OrderedLocusNames=RCAP_rcc00665; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodobacterales; Rhodobacter group; Rhodobacter. OX NCBI_TaxID=272942; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=8385667; DOI=10.1128/jb.175.8.2414-2422.1993; RA Burke D.H., Alberti M., Hearst J.E.; RT "bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and RT identification of the third subunit of light-independent RT protochlorophyllide reductase in bacteria and plants."; RL J. Bacteriol. 175:2414-2422(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=20418398; DOI=10.1128/jb.00366-10; RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., RA Haselkorn R.; RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium RT Rhodobacter capsulatus SB 1003."; RL J. Bacteriol. 192:3545-3546(2010). RN [3] RP CHARACTERIZATION. RC STRAIN=SB1003 / CB1029; RX PubMed=10811655; DOI=10.1074/jbc.m002904200; RA Fujita Y., Bauer C.E.; RT "Reconstitution of light-independent protochlorophyllide reductase from RT purified bchL and bchN-bchB subunits. In vitro confirmation of nitrogenase- RT like features of a bacteriochlorophyll biosynthesis enzyme."; RL J. Biol. Chem. 275:23583-23588(2000). RN [4] RP CHARACTERIZATION. RA Fujita Y.; RL Unpublished observations (JUL-2001). RN [5] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18358835; DOI=10.1016/j.febslet.2008.03.018; RA Nomata J., Ogawa T., Kitashima M., Inoue K., Fujita Y.; RT "NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is RT the catalytic component containing oxygen-tolerant Fe-S clusters."; RL FEBS Lett. 582:1346-1350(2008). RN [6] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH BCHB SUBUNIT AND 4FE-4S CLUSTER, RP FUNCTION, SUBUNIT, COFACTOR, REACTION MECHANISM, AND MUTAGENESIS OF PHE-25; RP CYS-26; CYS-51 AND CYS-112. RX PubMed=20400946; DOI=10.1038/nature08950; RA Muraki N., Nomata J., Ebata K., Mizoguchi T., Shiba T., Tamiaki H., RA Kurisu G., Fujita Y.; RT "X-ray crystal structure of the light-independent protochlorophyllide RT reductase."; RL Nature 465:110-114(2010). 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. {ECO:0000255|HAMAP-Rule:MF_00352, CC ECO:0000269|PubMed:18358835, ECO:0000269|PubMed:20400946}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 CC phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + CC 2 ATP + 2 H2O; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002, Rhea:RHEA- CC COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33722, CC ChEBI:CHEBI:33723, ChEBI:CHEBI:43474, ChEBI:CHEBI:83348, CC ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00352, CC ECO:0000269|PubMed:18358835}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00352, CC ECO:0000269|PubMed:20400946}; CC Note=Binds 1 [4Fe-4S] cluster per heterodimer (PubMed:20400946). The CC cluster is bound at the heterodimer interface by residues from both CC subunits (PubMed:20400946). {ECO:0000255|HAMAP-Rule:MF_00352, CC ECO:0000269|PubMed:20400946}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll CC biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00352}. 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 (PubMed:20400946). {ECO:0000255|HAMAP-Rule:MF_00352, CC ECO:0000269|PubMed:20400946}. CC -!- INTERACTION: CC P26164; P26163: bchB; NbExp=3; IntAct=EBI-9017544, EBI-9017546; CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|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; Z11165; CAA77526.1; -; Genomic_DNA. DR EMBL; CP001312; ADE84430.1; -; Genomic_DNA. DR PIR; B49851; B49851. DR RefSeq; WP_013066409.1; NC_014034.1. DR PDB; 3AEK; X-ray; 2.30 A; A/C=2-424. DR PDB; 3AEQ; X-ray; 2.90 A; A/C=2-424. DR PDB; 3AER; X-ray; 2.80 A; A/C=2-424. DR PDB; 3AES; X-ray; 2.50 A; A/C=2-424. DR PDB; 3AET; X-ray; 2.91 A; A/C=2-424. DR PDB; 3AEU; X-ray; 2.90 A; A/C=2-424. DR SMR; P26164; -. DR DIP; DIP-59277N; -. DR IntAct; P26164; 1. DR STRING; 272942.RCAP_rcc00665; -. DR GeneID; 31489611; -. DR KEGG; rcp:RCAP_rcc00665; -. DR eggNOG; COG2710; Bacteria. DR HOGENOM; CLU_037170_0_0_5; -. DR OMA; AAANFQC; -. DR OrthoDB; 5714774at2; -. DR BioCyc; MetaCyc:MONOMER-13269; -. DR BRENDA; 1.3.7.7; 5381. DR UniPathway; UPA00671; -. DR EvolutionaryTrace; P26164; -. DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3. DR HAMAP; MF_00352; ChlN_BchN; 1. DR InterPro; IPR050293; LIPOR_BchN/ChlN. DR InterPro; IPR000510; Nase/OxRdtase_comp1. DR InterPro; IPR005970; Protochl_reductN. 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. DR NCBIfam; TIGR01279; DPOR_bchN; 1. DR NCBIfam; NF002768; PRK02842.1; 1. 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: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:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro. DR Proteomes; UP000002361; Chromosome. DR AlphaFoldDB; P26164; -. DR MDposit; P26164; -. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis; KW Chlorophyll biosynthesis; Iron; Iron-sulfur; Metal-binding; KW Nucleotide-binding; Oxidoreductase; Photosynthesis; Reference proteome. FT CHAIN 1..424 FT /note="Light-independent protochlorophyllide reductase FT subunit N" FT /id="PRO_0000208596" FT BINDING 26 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000269|PubMed:20400946" FT BINDING 51 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000269|PubMed:20400946" FT BINDING 112 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000269|PubMed:20400946" FT MUTAGEN 25 FT /note="F->A: Retains 50% activity." FT /evidence="ECO:0000269|PubMed:20400946" FT MUTAGEN 26 FT /note="C->A: Does not form heterotetramers." FT /evidence="ECO:0000269|PubMed:20400946" FT MUTAGEN 51 FT /note="C->A: Does not form heterotetramers." FT /evidence="ECO:0000269|PubMed:20400946" FT MUTAGEN 112 FT /note="C->A: Does not form heterotetramers." FT /evidence="ECO:0000269|PubMed:20400946" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:3AEQ" FT STRAND 15..18 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 27..30 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 31..37 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 41..47 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 49..59 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 60..64 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 76..79 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 85..98 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 112..116 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 121..131 FT /evidence="ECO:0007829|PDB:3AEK" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 137..142 FT /evidence="ECO:0007829|PDB:3AEK" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 152..161 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 173..177 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 181..193 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 218..223 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 227..235 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:3AER" FT HELIX 248..262 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 267..286 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 289..292 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 301..304 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 306..315 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 320..327 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 331..338 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 346..350 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 353..363 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 366..370 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 372..379 FT /evidence="ECO:0007829|PDB:3AEK" FT TURN 380..382 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 388..391 FT /evidence="ECO:0007829|PDB:3AEK" FT STRAND 397..399 FT /evidence="ECO:0007829|PDB:3AEK" FT HELIX 402..420 FT /evidence="ECO:0007829|PDB:3AEK" SQ SEQUENCE 424 AA; 45830 MW; C90C75233802834D CRC64; MSLDSPTFGC TDSPVRRERG QKAVFCGLTS IVWLHRKMQD AFFLVVGSRT CAHLLQAAAG VMIFAEPRFG TAVLEEQDLA GLADAHKELD REVAKLLERR PDIRQLFLVG SCPSEVLKLD LDRAAERLSG LHAPHVRVYS YTGSGLDTTF TQGEDTCLAA MVPTLDTTEA AELIVVGALP DVVEDQCLSL LTQLGVGPVR MLPARRSDIE PAVGPNTRFI LAQPFLGETT GALERRGAKR IAAPFPFGEE GTTLWLKAVA DAYGVSAEKF EAVTAAPRAR AKKAIAAHLE TLTGKSLFMF PDSQLEIPLA RFLARECGMK TTEIATPFLH KAIMAPDLAL LPSNTALTEG QDLEAQLDRH EAINPDLTVC GLGLANPLEA KGHATKWAIE LVFTPVHFYE QAGDLAGLFS RPLRRRALLN GGAA //