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Database: UniProt/SWISS-PROT
Entry: CHLL_PROMM
LinkDB: CHLL_PROMM
Original site: CHLL_PROMM 
ID   CHLL_PROMM              Reviewed;         296 AA.
AC   Q7V6E7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   31-JUL-2019, entry version 108.
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=PMT_1217;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P.,
RA   Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R.,
RA   Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M.,
RA   Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A.,
RA   Webb E.A., Zinser E.R., Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic
RT   niche differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548175; CAE21392.1; -; Genomic_DNA.
DR   RefSeq; WP_011130587.1; NC_005071.1.
DR   SMR; Q7V6E7; -.
DR   STRING; 74547.PMT_1217; -.
DR   EnsemblBacteria; CAE21392; CAE21392; PMT_1217.
DR   KEGG; pmt:PMT_1217; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   KO; K04037; -.
DR   OMA; PGDIVCG; -.
DR   OrthoDB; 729012at2; -.
DR   BioCyc; PMAR74547:AKG35_RS06510-MONOMER; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000001423; 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_0000324063.
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;  32341 MW;  8C54E37DAEDC3413 CRC64;
     MTTTLTRPAD GEGSVQVQQD ASVRIQEGAL VIAVYGKGGI GKSTTSSNLS AAFSKLGKRV
     LQIGCDPKHD STFTLTHRMV PTVIDILEEV DFHSEELRPD DFMFEGFNGV KCVESGGPPA
     GTGCGGYVTG QTVKLLKEHH LLEDTDVVIF DVLGDVVCGG FAAPLQHANY CLIVTANDFD
     SIFAMNRIVA AINAKAKNYK VRLGGVIANR SAELDQIEKF NQQTGLKTMA HFKNVDAIRR
     SRLKKCTIFE MDSSDEGVME CQNEYLSLAQ KMLDNVEPLE AEPLKDREIF DLLGFD
//
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