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BCHN_CHLAA
ID   BCHN_CHLAA              Reviewed;         444 AA.
AC   Q9F6X6; A9WIN6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Caur_2557;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10976061; DOI=10.1126/science.289.5485.1724;
RA   Xiong J., Fischer W.M., Inoue K., Nakahara M., Bauer C.E.;
RT   "Molecular evidence for the early evolution of photosynthesis.";
RL   Science 289:1724-1730(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABY35763.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF288460; AAG15209.1; -; Genomic_DNA.
DR   EMBL; CP000909; ABY35763.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001636152.1; NC_010175.1.
DR   AlphaFoldDB; Q9F6X6; -.
DR   SMR; Q9F6X6; -.
DR   STRING; 324602.Caur_2557; -.
DR   EnsemblBacteria; ABY35763; ABY35763; Caur_2557.
DR   KEGG; cau:Caur_2557; -.
DR   PATRIC; fig|324602.8.peg.2882; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_037170_0_0_0; -.
DR   InParanoid; Q9F6X6; -.
DR   OMA; ISCVAWL; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000002008; Chromosome.
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; Reference proteome.
FT   CHAIN           1..444
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit N"
FT                   /id="PRO_0000208593"
FT   BINDING         36
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         61
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         118
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   444 AA;  48746 MW;  D696C7E3AE735339 CRC64;
     MFLNPVVPNG YYNLRGGAMQ SKATPIREDG IYHSFCGLVS VGWLYQKIKD SFFLILGTHT
     CAHLLQNTLG VMIFARPRFA VSLLEESDLS SSQPDISAQI EEIKREHHPS VIFLLSSCTP
     EVMKVEFEGL AASVSTPEVP VLFVPASGLD YTFSQSEDSV LQALIPFCPP APPDDKRVVF
     LGSVNDAIAD DFSLEAARLG IPVAGFLPAS HFTELPPIGP GTVIAPLQPY LHKTATQLRN
     ERGCTVLSSL FPFGPDGTRR FWEDLAAQFG MQVDLSEREA AAWERIKHHT DLLRGKKIFF
     ASDTLMELPL ARFLKACGAE VVECSTPYIN RRFHAAELAA LDGVRLVEQA NFHRQLRTIT
     ETKPDLIISN IITTNPLVGQ GTVAKWGTEY CFLPIHGWAG VNNLVTSFTR ALQRHARLDP
     LGSDPIWLTG MMPGSSGGVI SLQS
 
 
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