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BCHN_CHLCH
ID   BCHN_CHLCH              Reviewed;         427 AA.
AC   Q3APK9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=bchN {ECO:0000255|HAMAP-Rule:MF_00352}; OrderedLocusNames=Cag_1815;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; 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. {ECO:0000255|HAMAP-Rule:MF_00352}.
CC   -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|HAMAP-
CC       Rule:MF_00352}.
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DR   EMBL; CP000108; ABB29066.1; -; Genomic_DNA.
DR   RefSeq; WP_011362828.1; NC_007514.1.
DR   AlphaFoldDB; Q3APK9; -.
DR   SMR; Q3APK9; -.
DR   STRING; 340177.Cag_1815; -.
DR   EnsemblBacteria; ABB29066; ABB29066; Cag_1815.
DR   KEGG; cch:Cag_1815; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_037170_0_0_10; -.
DR   OMA; ISCVAWL; -.
DR   OrthoDB; 363662at2; -.
DR   UniPathway; UPA00671; -.
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:0036070; P:light-independent bacteriochlorophyll 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; Bacteriochlorophyll biosynthesis;
KW   Chlorophyll biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Oxidoreductase; Photosynthesis.
FT   CHAIN           1..427
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit N"
FT                   /id="PRO_0000324002"
FT   BINDING         25
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         50
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   427 AA;  47373 MW;  0C5812F2FB3A3023 CRC64;
     MMQGIGGDIQ DSQLIREDNV THSFCGLACV GWMYQKIKDS FFLILGTHTC AHFLQNALGM
     MIFAKPRFGI ALIEEGDLAK NEPTLQEVVS EIKADHHPSV IFLLSSCTPE VMKVDFKGLA
     DHLSTPETPV LFVPASGLVY NFTQAEDSIL SALVPYCPQA PAGEKKVVFL GSVNDSTAAD
     IRADAEELGI PVGGFLPESR FDKMPAIGPD TVLAPIQPYL SRVALKLSRE RGSTVLHSLF
     PYGPDGSRVF WEDLAREFGI TVDLREREAA AWEKIRKQTD KLKGKKVFLT ADTMLELPLA
     RFLRHAGADI MECSSAYIIK KFHAKELEAL QGVRVVEQPN FHRQLEDIRR ERPDLIVTSL
     MTANPFVGNG FVVKWSMEFM LMPIHSWSGV VSLANLFVAP LQRRSMLPAF DESVWLEGAM
     PSAEVHA
 
 
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