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Database: UniProt/SWISS-PROT
Entry: CHLL_PROMA
LinkDB: CHLL_PROMA
Original site: CHLL_PROMA 
ID   CHLL_PROMA              Reviewed;         296 AA.
AC   Q7VD39;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   31-JUL-2019, entry version 102.
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=Pro_0544;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F.,
RA   Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B.,
RA   Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P.,
RA   Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120,
RT   a nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAP99589.1; -; Genomic_DNA.
DR   RefSeq; NP_874937.1; NC_005042.1.
DR   RefSeq; WP_011124698.1; NC_005042.1.
DR   PDB; 2YNM; X-ray; 2.10 A; A/B=1-296.
DR   PDBsum; 2YNM; -.
DR   SMR; Q7VD39; -.
DR   STRING; 167539.Pro_0544; -.
DR   PRIDE; Q7VD39; -.
DR   EnsemblBacteria; AAP99589; AAP99589; Pro_0544.
DR   GeneID; 1461926; -.
DR   KEGG; pma:Pro_0544; -.
DR   PATRIC; fig|167539.5.peg.559; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   KO; K04037; -.
DR   OMA; PGDIVCG; -.
DR   OrthoDB; 729012at2; -.
DR   BioCyc; PMAR167539:G1G0G-562-MONOMER; -.
DR   BRENDA; 1.3.1.33; 5023.
DR   BRENDA; 1.3.7.7; 5023.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000001420; 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   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; ATP-binding; Chlorophyll biosynthesis;
KW   Complete proteome; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW   Nucleotide-binding; Oxidoreductase; Photosynthesis;
KW   Reference proteome.
FT   CHAIN         1    296       Light-independent protochlorophyllide
FT                                reductase iron-sulfur ATP-binding
FT                                protein.
FT                                /FTId=PRO_0000324057.
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}.
FT   STRAND       30     37       {ECO:0000244|PDB:2YNM}.
FT   HELIX        42     55       {ECO:0000244|PDB:2YNM}.
FT   STRAND       60     66       {ECO:0000244|PDB:2YNM}.
FT   HELIX        73     76       {ECO:0000244|PDB:2YNM}.
FT   HELIX        83     89       {ECO:0000244|PDB:2YNM}.
FT   TURN         90     92       {ECO:0000244|PDB:2YNM}.
FT   HELIX        94     96       {ECO:0000244|PDB:2YNM}.
FT   HELIX        99    102       {ECO:0000244|PDB:2YNM}.
FT   HELIX       107    109       {ECO:0000244|PDB:2YNM}.
FT   STRAND      111    114       {ECO:0000244|PDB:2YNM}.
FT   STRAND      122    124       {ECO:0000244|PDB:2YNM}.
FT   HELIX       125    138       {ECO:0000244|PDB:2YNM}.
FT   TURN        139    143       {ECO:0000244|PDB:2YNM}.
FT   STRAND      144    152       {ECO:0000244|PDB:2YNM}.
FT   HELIX       159    161       {ECO:0000244|PDB:2YNM}.
FT   HELIX       163    166       {ECO:0000244|PDB:2YNM}.
FT   STRAND      169    175       {ECO:0000244|PDB:2YNM}.
FT   HELIX       179    195       {ECO:0000244|PDB:2YNM}.
FT   TURN        196    198       {ECO:0000244|PDB:2YNM}.
FT   STRAND      202    210       {ECO:0000244|PDB:2YNM}.
FT   HELIX       215    224       {ECO:0000244|PDB:2YNM}.
FT   STRAND      228    232       {ECO:0000244|PDB:2YNM}.
FT   HELIX       236    243       {ECO:0000244|PDB:2YNM}.
FT   HELIX       248    250       {ECO:0000244|PDB:2YNM}.
FT   HELIX       258    274       {ECO:0000244|PDB:2YNM}.
FT   HELIX       286    292       {ECO:0000244|PDB:2YNM}.
SQ   SEQUENCE   296 AA;  32395 MW;  D46A27CE10432012 CRC64;
     MTTTLANRPD GEGSVQVKLD PKVNIEEGAL VIAVYGKGGI GKSTTSSNLS AAFSKLGKKV
     LQIGCDPKHD STFTLTHKMV PTVIDILEEV DFHSEELRPQ DFMFEGFNGV QCVESGGPPA
     GTGCGGYVTG QTVKLLKEHH LLEDTDVVIF DVLGDVVCGG FAAPLQHANY CLIVTANDFD
     SIFAMNRIVA AINAKAKNYK VRLGGVIANR SAELDQIEKF NEKTGLKTMA HFRNVDAIRR
     SRLKKCTIFE MDPEEEGVLE VQNEYLSLAK KMIDNVEPLE AEPLKDREIF DLLGFD
//
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