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Database: UniProt
Entry: CHLL_THEEB
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Original site: CHLL_THEEB 
ID   CHLL_THEEB              Reviewed;         281 AA.
AC   Q8DGH0;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   28-MAR-2018, entry version 109.
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=tll2347;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
RA   Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC09899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BA000039; BAC09899.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_683137.1; NC_004113.1.
DR   ProteinModelPortal; Q8DGH0; -.
DR   SMR; Q8DGH0; -.
DR   STRING; 197221.tll2347; -.
DR   EnsemblBacteria; BAC09899; BAC09899; BAC09899.
DR   GeneID; 1011941; -.
DR   KEGG; tel:tll2347; -.
DR   PATRIC; fig|197221.4.peg.2460; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   HOGENOM; HOG000228825; -.
DR   KO; K04037; -.
DR   OMA; PGDIVCG; -.
DR   OrthoDB; POG091H0230; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0036068; P:light-independent chlorophyll 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; ATP-binding; Chlorophyll biosynthesis; Complete proteome;
KW   Iron; Iron-sulfur; Magnesium; Metal-binding; Nucleotide-binding;
KW   Oxidoreductase; Photosynthesis; Reference proteome.
FT   CHAIN         1    281       Light-independent protochlorophyllide
FT                                reductase iron-sulfur ATP-binding
FT                                protein.
FT                                /FTId=PRO_0000139571.
FT   NP_BIND      10     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     180    181       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   METAL        14     14       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL        95     95       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       129    129       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   BINDING      39     39       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
SQ   SEQUENCE   281 AA;  30542 MW;  F1C4628BF6134630 CRC64;
     MKLAVYGKGG IGKSTTSCNI SVALARRGKK VLQIGCDPKH DSTFTLTGFL IPTIIDTLQA
     KDYHYEDVWP EDVIYKGYGG VDCVEAGGPP AGAGCGGYVV GETVKLLKEL NAFDEYDVIL
     FDVLGDVVCG GFAAPLNYAD YCLIVTDNGF DALFAANRIA ASVREKARTH PLRLAGLIGN
     RTNKRDLIEK YVEAVPMPIL EVLPLIEDIR VSRVKGKTLF EMAESDPSLN DVCDYYLNIA
     DQILARPEGV VPKDVPDRDL FALLSDFYLN PQGSERSLAA V
//
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