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Database: UniProt/SWISS-PROT
Entry: BCHL_RHORT
LinkDB: BCHL_RHORT
Original site: BCHL_RHORT 
ID   BCHL_RHORT              Reviewed;         295 AA.
AC   Q2RWS1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   31-JUL-2019, entry version 84.
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=Rru_A0620;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG
OS   4362 / NCIB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N.C., Mavromatis K., Richardson P., Rohde M., Goeker M.,
RA   Klenk H.P., Zhang Y., Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC21424.1; -; Genomic_DNA.
DR   RefSeq; WP_011388378.1; NC_007643.1.
DR   RefSeq; YP_425711.1; NC_007643.1.
DR   SMR; Q2RWS1; -.
DR   STRING; 269796.Rru_A0620; -.
DR   EnsemblBacteria; ABC21424; ABC21424; Rru_A0620.
DR   GeneID; 3834356; -.
DR   KEGG; rru:Rru_A0620; -.
DR   PATRIC; fig|269796.9.peg.675; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   HOGENOM; HOG000228825; -.
DR   KO; K04037; -.
DR   OMA; EVDFHHE; -.
DR   OrthoDB; 729012at2; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000001929; 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    295       Light-independent protochlorophyllide
FT                                reductase iron-sulfur ATP-binding
FT                                protein.
FT                                /FTId=PRO_0000324073.
FT   NP_BIND      39     44       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     209    210       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     233    235       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   METAL        43     43       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       124    124       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       158    158       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   BINDING      68     68       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
SQ   SEQUENCE   295 AA;  32108 MW;  23902EEE828057DA CRC64;
     MFDETMRQPP DGEGSVQVEM DPALHIETAK VFAIYGKGGI GKSTTSSNLS AAFSKLGKRV
     VQIGCDPKHD STFTLTKRLV PTVIDVLQAV HFHTEELRVE DFVYEGYNGV MCVEAGGPPA
     GTGCGGYVVG QTVKLLKEHH ILEDADVVVF DVLGDVVCGG FATPLQHAER ALVVAANDFD
     SIFAANRIAA AIQAKAKNYD VRLGGIIANR SVATDQIERF NARSGMRTLA HFPDLDVIRR
     SRLCKSTLFE MEPSPELAAV QQEYLRLAEA LWEGVEPLTA TPLIDREIFD LLGFD
//
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