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BCHL_CHLP8
ID   BCHL_CHLP8              Reviewed;         276 AA.
AC   B3QQZ4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein {ECO:0000255|HAMAP-Rule:MF_00355};
DE            Short=DPOR subunit L {ECO:0000255|HAMAP-Rule:MF_00355};
DE            Short=LI-POR subunit L {ECO:0000255|HAMAP-Rule:MF_00355};
DE            EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00355};
GN   Name=bchL {ECO:0000255|HAMAP-Rule:MF_00355}; OrderedLocusNames=Cpar_0221;
OS   Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS   subsp. thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 263 / NCIMB 8327;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-2008) 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 L component serves as a unique
CC       electron donor to the NB-component of the complex, and binds Mg-ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_00355}.
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_00355};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00355};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000255|HAMAP-
CC       Rule:MF_00355};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC       biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00355}.
CC   -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of three
CC       subunits; BchL, BchN and BchB. {ECO:0000255|HAMAP-Rule:MF_00355}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000255|HAMAP-
CC       Rule:MF_00355}.
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DR   EMBL; CP001099; ACF10648.1; -; Genomic_DNA.
DR   RefSeq; WP_012501482.1; NC_011027.1.
DR   AlphaFoldDB; B3QQZ4; -.
DR   SMR; B3QQZ4; -.
DR   STRING; 517417.Cpar_0221; -.
DR   EnsemblBacteria; ACF10648; ACF10648; Cpar_0221.
DR   KEGG; cpc:Cpar_0221; -.
DR   eggNOG; COG1348; Bacteria.
DR   HOGENOM; CLU_059373_2_0_10; -.
DR   OMA; EVDFHHE; -.
DR   OrthoDB; 729012at2; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000008811; 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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00355; ChlL_BchL; 1.
DR   InterPro; IPR030655; NifH/chlL_CS.
DR   InterPro; IPR000392; NifH/frxC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005971; Protochlorophyllide_ATP-bd.
DR   PANTHER; PTHR42864; PTHR42864; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01281; DPOR_bchL; 1.
DR   PROSITE; PS00746; NIFH_FRXC_1; 1.
DR   PROSITE; PS00692; NIFH_FRXC_2; 1.
DR   PROSITE; PS51026; NIFH_FRXC_3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
KW   Chlorophyll biosynthesis; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW   Nucleotide-binding; Oxidoreductase; Photosynthesis.
FT   CHAIN           1..276
FT                   /note="Light-independent protochlorophyllide reductase
FT                   iron-sulfur ATP-binding protein"
FT                   /id="PRO_1000120551"
FT   BINDING         12..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT   BINDING         97
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT   BINDING         131
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT   BINDING         182..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
SQ   SEQUENCE   276 AA;  29512 MW;  7BB1B06DEBB1E4C5 CRC64;
     MSLVLAVYGK GGIGKSTTSA NISAALALKG AKVLQIGCDP KHDSTFPITG KLQKTVIEAL
     EEVDFHHEEL SPEDIVETGF AGIDGLEAGG PPAGSGCGGY VVGESVTLLQ EMGLYDKYDV
     ILFDVLGDVV CGGFSAPLNY ADYAVIIATN DFDSIFAANR LCMAIQQKSV RYKVQLAGIV
     ANRVDYTKGG GTNMLDQFAE QVGTRLLAKV PYHELIRKSR FAGKTLFAMD ENEPELADCL
     APYNEIAEQI LSKTPIASVP KPIGDREIFD IVGGWQ
 
 
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