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Database: UniProt/SWISS-PROT
Entry: BCHL_RHOPA
LinkDB: BCHL_RHOPA
Original site: BCHL_RHOPA 
ID   BCHL_RHOPA              Reviewed;         312 AA.
AC   Q6N9K0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   31-JUL-2019, entry version 96.
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};
GN   OrderedLocusNames=RPA1545;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile
RT   photosynthetic bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
CC   -!- FUNCTION: Component of the dark-operative protochlorophyllide
CC       reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce
CC       ring D of protochlorophyllide (Pchlide) to form chlorophyllide a
CC       (Chlide). This reaction is light-independent. The L component
CC       serves as a unique electron donor to the NB-component of the
CC       complex, and binds Mg-ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-
CC         [ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide
CC         a + reduced 2[4Fe-4S]-[ferredoxin]; Xref=Rhea:RHEA:28202,
CC         Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83348, ChEBI:CHEBI:83350,
CC         ChEBI:CHEBI:456216; EC=1.3.7.7; Evidence={ECO:0000255|HAMAP-
CC         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;
CC       bacteriochlorophyll biosynthesis (light-independent).
CC       {ECO:0000255|HAMAP-Rule:MF_00355}.
CC   -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of
CC       three subunits; BchL, BchN and BchB. {ECO:0000255|HAMAP-
CC       Rule:MF_00355}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000255|HAMAP-Rule:MF_00355}.
DR   EMBL; BX572597; CAE26986.1; -; Genomic_DNA.
DR   RefSeq; WP_011157104.1; NC_005296.1.
DR   SMR; Q6N9K0; -.
DR   STRING; 258594.RPA1545; -.
DR   PRIDE; Q6N9K0; -.
DR   EnsemblBacteria; CAE26986; CAE26986; RPA1545.
DR   KEGG; rpa:RPA1545; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   HOGENOM; HOG000228825; -.
DR   KO; K04037; -.
DR   OMA; EVDFHHE; -.
DR   PhylomeDB; Q6N9K0; -.
DR   BioCyc; RPAL258594:TX73_RS07875-MONOMER; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000001426; 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_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   PANTHER; PTHR42864:SF1; PTHR42864:SF1; 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; Complete proteome; Iron; Iron-sulfur;
KW   Magnesium; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW   Photosynthesis; Reference proteome.
FT   CHAIN         1    312       Light-independent protochlorophyllide
FT                                reductase iron-sulfur ATP-binding
FT                                protein.
FT                                /FTId=PRO_0000324068.
FT   NP_BIND      55     60       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     225    226       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     249    251       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   METAL        59     59       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       140    140       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       174    174       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   BINDING      84     84       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
SQ   SEQUENCE   312 AA;  33898 MW;  3DAF953D391FCAA6 CRC64;
     MNILTDPNKL KTSGCADVNA SKCAEGDGEG SVQVQLDPNL NIGTAKVFSI YGKGGIGKST
     TSSNLSVAFS KLGKRVLQIG CDPKHDSTFT LTKKLMPTVI DVLESVNFHS EEVRPEDFVF
     EGYNGVMCVE AGGPPAGTGC GGYVVGQTVK LLKEHHLLED TDVVIFDVLG DVVCGGFASP
     LQHSERAMIV AANDFDSIFA ANRIAAAIQA KSKNYAVRLA GVIANRSRET DQIDKFGERT
     GIKRVAHLPD LDVIRKSRLK KMTLFEMDHT PEIEAVQNEY LRLATELWEA KEPPVQGKPL
     KDRDIFDLLG FD
//
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