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Database: UniProt/SWISS-PROT
Entry: BCHL_DINSH
LinkDB: BCHL_DINSH
Original site: BCHL_DINSH 
ID   BCHL_DINSH              Reviewed;         299 AA.
AC   A8LQ30;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   31-JUL-2019, 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=Dshi_3537;
OS   Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16493 / NCIMB 14021 / DFL 12;
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S.,
RA   Han C., Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N.,
RA   Liebl W., Liesegang H., Meincke L., Pati A., Petersen J.,
RA   Piekarski T., Pommerenke C., Pradella S., Pukall R., Rabus R.,
RA   Stackebrandt E., Thole S., Thompson L., Tielen P., Tomasch J.,
RA   von Jan M., Wanphrut N., Wichels A., Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter
RT   shibae: a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
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; CP000830; ABV95270.1; -; Genomic_DNA.
DR   RefSeq; WP_012180193.1; NC_009952.1.
DR   SMR; A8LQ30; -.
DR   STRING; 398580.Dshi_3537; -.
DR   EnsemblBacteria; ABV95270; ABV95270; Dshi_3537.
DR   KEGG; dsh:Dshi_3537; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   HOGENOM; HOG000228825; -.
DR   KO; K04037; -.
DR   OMA; EVDFHHE; -.
DR   OrthoDB; 729012at2; -.
DR   BioCyc; DSHI398580:G1GA2-3598-MONOMER; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000006833; 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    299       Light-independent protochlorophyllide
FT                                reductase iron-sulfur ATP-binding
FT                                protein.
FT                                /FTId=PRO_0000324054.
FT   NP_BIND      43     48       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     213    214       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     237    239       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   METAL        47     47       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       128    128       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       162    162       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   BINDING      72     72       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
SQ   SEQUENCE   299 AA;  32557 MW;  52564A7F3C83DF5E CRC64;
     MSPLDTAPPV LKGEDGEGSV QVHQDDSMKI EGAKVFSVYG KGGIGKSTTS SNLSAAFSKL
     GKRVLQIGCD PKHDSTFTLT GSLVPTVIDI LKEVDFHAEE LRPEDFVFEG FNGVKCVEAG
     GPPAGTGCGG YVVGQTVKLL KQHHLLEDTD VVIFDVLGDV VCGGFAAPLQ HADRALIVTA
     NDFDSIYAMN RIIAAVQAKS KNYSVRLAGC VANRSRETDE VDRYCKTVGF NRIAHMPDLD
     AIRRSRLKKK TLFEMEDAED VVQVRKEYIR LAETLWNGTE PLAPAPLPDR EIFELLGFD
//
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