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Database: UniProt
Entry: A0A0P0LG75_9BURK
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ID   A0A0P0LG75_9BURK        Unreviewed;       303 AA.
AC   A0A0P0LG75;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-MAR-2018, entry version 16.
DE   RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein {ECO:0000256|HAMAP-Rule:MF_00355};
DE            Short=DPOR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
DE            Short=LI-POR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
DE            EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00355};
GN   Name=chlL {ECO:0000313|EMBL:ALK87882.1};
GN   Synonyms=bchL {ECO:0000256|HAMAP-Rule:MF_00355};
GN   ORFNames=L63ED372_00655 {ECO:0000313|EMBL:ALK87882.1};
OS   Limnohabitans sp. 63ED37-2.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK87882.1, ECO:0000313|Proteomes:UP000059510};
RN   [1] {ECO:0000313|EMBL:ALK87882.1, ECO:0000313|Proteomes:UP000059510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK87882.1,
RC   ECO:0000313|Proteomes:UP000059510};
RA   Ahn J.-H., Kim S.B.;
RT   "Limnohabitans sp. 2 strains.";
RL   Submitted (JUN-2015) 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:0000256|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:0000256|HAMAP-Rule:MF_00355}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00355};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000256|HAMAP-
CC       Rule:MF_00355};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism;
CC       bacteriochlorophyll biosynthesis (light-independent).
CC       {ECO:0000256|HAMAP-Rule:MF_00355}.
CC   -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of
CC       three subunits; BchL, BchN and BchB. {ECO:0000256|HAMAP-
CC       Rule:MF_00355}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000256|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688}.
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DR   EMBL; CP011774; ALK87882.1; -; Genomic_DNA.
DR   RefSeq; WP_062403277.1; NZ_CP011774.1.
DR   EnsemblBacteria; ALK87882; ALK87882; L63ED372_00655.
DR   KEGG; lih:L63ED372_00655; -.
DR   PATRIC; fig|1678128.3.peg.656; -.
DR   KO; K04037; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000059510; 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   CDD; cd02032; Bchl_like; 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   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 {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000313|EMBL:ALK87882.1};
KW   Bacteriochlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Chlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Complete proteome {ECO:0000313|Proteomes:UP000059510};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000313|EMBL:ALK87882.1};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059510}.
FT   NP_BIND      47     52       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
FT   NP_BIND     217    218       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
FT   NP_BIND     241    243       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
FT   METAL        51     51       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00355}.
FT   METAL       132    132       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00355}.
FT   METAL       166    166       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00355}.
FT   BINDING      76     76       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
SQ   SEQUENCE   303 AA;  32829 MW;  ED0A98F07772C012 CRC64;
     MIETTSIPVN SIQRVRGADG EGSVQFQMDP TVKIGTAKVF AVYGKGGIGK STTSSNLSVA
     FSKLGKRVLQ IGCDPKHDST FTLTKKLMPT VIDALETVDF HAEELRLDDF VFKGYNGVMC
     VEAGGPPAGT GCGGYVVGQT VKLLKEHHLL EDTDVVIFDV LGDVVCGGFA APLQHADRAL
     IVTANDFDSI FAMNRIVQAI GAKAKNYNVR LGGVIANRSD ATDQIDKYNA VTGLKTMAHF
     PMLDEIRKSR LQKCTLFELE PTPAVKAVQD EYMRLAEALW LGADPLPSIP MKDRDIFDLL
     GFD
//
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