ID BCHL_RHOPS Reviewed; 312 AA.
AC Q132N5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 02-NOV-2016, entry version 73.
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=RPD_3733;
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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: Protochlorophyllide a + reduced ferredoxin + 2
CC ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2
CC phosphate. {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;
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; CP000283; ABE40954.1; -; Genomic_DNA.
DR RefSeq; WP_011504119.1; NC_007958.1.
DR ProteinModelPortal; Q132N5; -.
DR STRING; 316057.RPD_3733; -.
DR EnsemblBacteria; ABE40954; ABE40954; RPD_3733.
DR KEGG; rpd:RPD_3733; -.
DR PATRIC; 23282627; VBIRhoPal120395_3867.
DR eggNOG; ENOG4105DSM; Bacteria.
DR eggNOG; COG1348; LUCA.
DR HOGENOM; HOG000228825; -.
DR KO; K04037; -.
DR OMA; TSCNISV; -.
DR OrthoDB; POG091H0230; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000001818; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
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-HAMAP.
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; Nitogenase_NifH/Reductase_ChlL.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005971; Protochlorophyllide_ATP-bd.
DR PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR PRINTS; PR00091; NITROGNASEII.
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.
FT CHAIN 1 312 Light-independent protochlorophyllide
FT reductase iron-sulfur ATP-binding
FT protein.
FT /FTId=PRO_0000324071.
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}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 167 180 ipat:NIFH_FRXC_2 [T]
FT MYHIT 46 312 ihamap:ChlL_BchL [T]
FT MYHIT 45 312 iprf:NIFH_FRXC_3 [T]
FT MYHIT 130 142 ipat:NIFH_FRXC_1 [T]
FT MYHIT 48 309 ipfam:Fer4_NifH [T]
SQ SEQUENCE 312 AA; 33897 MW; BD941FE6C88E458C CRC64;
MNILTDPLKL KTSGCADANA SKCAEGDGEG SVQVQLDPNV KIGSAKVFSI YGKGGIGKST
TSSNLSVAFS KLGKRVLQIG CDPKHDSTFT LTKRLIPTVI DVLEEVNFHS EELRPEDFVF
EGYNGVMCLE AGGPPAGTGC GGYVVGQTVK LLKEHHLLED TDVVIFDVLG DVVCGGFAAP
LQHSERAMIV AANDFDSIFA ANRIAAAIAA KSKNYGVRLG GIIANRSKDT DQIDKFGERT
GIRRIAHLPD LDVIRKSRLK KMTLFEMDHT DEILAVQQEY LRLATEMWEA KEPPIEGKPL
KDRDIFDLLG FD
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