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Database: UniProt/SWISS-PROT
Entry: CHLL_SYNS3
LinkDB: CHLL_SYNS3
Original site: CHLL_SYNS3 
ID   CHLL_SYNS3              Reviewed;         296 AA.
AC   Q0I8P4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   31-JUL-2019, entry version 92.
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=chlL {ECO:0000255|HAMAP-Rule:MF_00355};
GN   OrderedLocusNames=sync_1975;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F.,
RA   Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J.,
RA   Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y.,
RA   Halpin R., Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to
RT   a coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; chlorophyll
CC       biosynthesis (light-independent). {ECO:0000255|HAMAP-
CC       Rule:MF_00355}.
CC   -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of
CC       three subunits; ChlL, ChlN and ChlB. {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; CP000435; ABI46262.1; -; Genomic_DNA.
DR   RefSeq; WP_011619890.1; NC_008319.1.
DR   SMR; Q0I8P4; -.
DR   STRING; 64471.sync_1975; -.
DR   EnsemblBacteria; ABI46262; ABI46262; sync_1975.
DR   KEGG; syg:sync_1975; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   HOGENOM; HOG000228825; -.
DR   KO; K04037; -.
DR   OMA; PGDIVCG; -.
DR   OrthoDB; 729012at2; -.
DR   BioCyc; SSP64471:G1G72-1841-MONOMER; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000001961; 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:0036068; P:light-independent chlorophyll 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; Chlorophyll biosynthesis; Complete proteome;
KW   Iron; Iron-sulfur; Magnesium; Metal-binding; Nucleotide-binding;
KW   Oxidoreductase; Photosynthesis; Reference proteome.
FT   CHAIN         1    296       Light-independent protochlorophyllide
FT                                reductase iron-sulfur ATP-binding
FT                                protein.
FT                                /FTId=PRO_0000324075.
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   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   296 AA;  32334 MW;  0377B4922CBFBA3D CRC64;
     MTTTLTRPAD GDGSVQVHQD PGTKIEEGAL VIAVYGKGGI GKSTTSSNLS AAFSKLGKRV
     LQIGCDPKHD STFTLTHKMV PTVIDILEEV DFHSEELRPE DFMFTGYNGV KCVESGGPPA
     GTGCGGYVTG QTVKLLKEHH LLEDTDVVIF DVLGDVVCGG FAAPLQHANY CLIVTANDFD
     SIFAMNRIVQ AIQAKAKNYK VRLGGVVANR SAETDQIDKF NERTGLRTMA HFKDVDAIRR
     SRLKKCTIFE MDDKDDGVKA VQDEYIRLAS NMLNNVEPLE AVSLKDREIF DLLGFD
//
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