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CHLN_GLOVI
ID   CHLN_GLOVI              Reviewed;         469 AA.
AC   Q7NI15;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=gll2369;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(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   -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|HAMAP-
CC       Rule:MF_00352}.
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DR   EMBL; BA000045; BAC90310.1; -; Genomic_DNA.
DR   RefSeq; NP_925315.1; NC_005125.1.
DR   RefSeq; WP_011142365.1; NC_005125.1.
DR   AlphaFoldDB; Q7NI15; -.
DR   SMR; Q7NI15; -.
DR   STRING; 251221.35212937; -.
DR   EnsemblBacteria; BAC90310; BAC90310; BAC90310.
DR   KEGG; gvi:gll2369; -.
DR   PATRIC; fig|251221.4.peg.2408; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_037170_0_0_3; -.
DR   InParanoid; Q7NI15; -.
DR   OMA; ISCVAWL; -.
DR   OrthoDB; 363662at2; -.
DR   PhylomeDB; Q7NI15; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000000557; 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: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   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding; Oxidoreductase; Photosynthesis;
KW   Reference proteome.
FT   CHAIN           1..469
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit N"
FT                   /id="PRO_0000208600"
FT   BINDING         24
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         49
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         109
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   469 AA;  52747 MW;  86C09B347B4195BE CRC64;
     MVSQPTTSSG PQFECETGNY HTFCPISCVA WLYQKIEDSF FLVIGTKTCG YFLQNAMGVM
     IFAEPRYAMA ELEEGDVNAK LNAYDELQRL CLQVKKDRNP SVIVWIGTCT TEIIKMDLEG
     IAPKLEDEIG IPIVVARANG LDYAFTQGED TVLAAMASRC PAPQEVRSEE EKKERTGGLR
     TLFSHGKKDE KKAGPAPSEY VDHQPLVLFG SLTDPVVNQL TLELKKQGIR VSGWLPAPRY
     TELPIVEQGV TYVAGVNPFL SRTASALQRR MRCNLITTPF PIGPDGTRGW IEAICQALGV
     IPKGLDEREQ QIWDALRDDV EFLKGRSVFF MGDNLLEVSM ARFLIRCGMI VHEVGIPYMD
     KRYQQAELEL LDRTCRELGH PPVRIVEKPD NYNQIQRIYA CKPDLVITGM AHANPLEARG
     ITTKWSVEFT FAMIHGFTNA HDMLKMVRKP LDRNNALKSL GWEKLIQEV
 
 
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