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Database: UniProt/SWISS-PROT
Entry: BCHL_RUBGI
LinkDB: BCHL_RUBGI
Original site: BCHL_RUBGI 
ID   BCHL_RUBGI              Reviewed;         302 AA.
AC   Q9JPA5; I0HUK1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   31-JUL-2019, entry version 103.
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=RGE_33490;
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Rubrivivax.
OX   NCBI_TaxID=983917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144;
RX   PubMed=11343129; DOI=10.1007/s002390010163;
RA   Igarashi N., Harada J., Nagashima S., Matsuura K., Shimada K.,
RA   Nagashima K.V.P.;
RT   "Horizontal transfer of the photosynthesis gene cluster and operon
RT   rearrangement in purple bacteria.";
RL   J. Mol. Evol. 52:333-341(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144;
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-Isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S.,
RA   Fujita N., Shimada K., Hanada S., Nagashima K.V.;
RT   "Complete genome sequence of phototrophic betaproteobacterium
RT   Rubrivivax gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(2012).
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; AB034704; BAA94056.1; -; Genomic_DNA.
DR   EMBL; AP012320; BAL96688.1; -; Genomic_DNA.
DR   PIR; T50903; T50903.
DR   RefSeq; WP_014429549.1; NC_017075.1.
DR   SMR; Q9JPA5; -.
DR   STRING; 983917.RGE_33490; -.
DR   EnsemblBacteria; BAL96688; BAL96688; RGE_33490.
DR   KEGG; rge:RGE_33490; -.
DR   PATRIC; fig|983917.3.peg.3275; -.
DR   KO; K04037; -.
DR   OMA; EVDFHHE; -.
DR   OrthoDB; 729012at2; -.
DR   BioCyc; RGEL983917:G1H8K-3286-MONOMER; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000007883; 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    302       Light-independent protochlorophyllide
FT                                reductase iron-sulfur ATP-binding
FT                                protein.
FT                                /FTId=PRO_0000139580.
FT   NP_BIND      46     51       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     216    217       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     240    242       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   METAL        50     50       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       131    131       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       165    165       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   BINDING      75     75       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
SQ   SEQUENCE   302 AA;  32658 MW;  CD3DFFFA24FDAAE7 CRC64;
     MSTATISPSQ IGRGARPDGE GSVQVQMETG AKIGNAKVFA IYGKGGIGKS TTSSNLSVAF
     SKLGKRVLQI GCDPKHDSTF TLTKRMVPTV IDVLETVNFH PEELRVEDFV FEGTNGVMCV
     EAGGPPAGTG CGGYVVGQTV KLLKEHHLLE ETDVVVFDVL GDVVCGGFAA PLQHADRALI
     VTANDFDSIF AANRIVQAIG AKAKNYNVRL GGIIANRSDA TDQIDKFNER IGMRSLARIP
     ALDVIRKSRL KKATLFEMEE SPEVLAVQAE YLQLAQRLWD GVDPLYCEPL KDRDIFDLLG
     YD
//
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