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 03-AUG-2022, entry version 115.
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}; OrderedLocusNames=Pro_0544;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
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., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
CC -!- FUNCTION: Component of the dark-operative protochlorophyllide reductase
CC (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of
CC protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This
CC reaction is light-independent. The L component serves as a unique
CC electron donor to the NB-component of the complex, and binds Mg-ATP.
CC {ECO:0000255|HAMAP-Rule:MF_00355}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2
CC phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-
CC 4S]-[ferredoxin]; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002,
CC Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83348, ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7;
CC Evidence={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-Rule:MF_00355}.
CC -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of three
CC subunits; ChlL, ChlN and ChlB. {ECO:0000255|HAMAP-Rule:MF_00355}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000255|HAMAP-
CC Rule:MF_00355}.
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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 AlphaFoldDB; Q7VD39; -.
DR SMR; Q7VD39; -.
DR IntAct; Q7VD39; 1.
DR STRING; 167539.Pro_0544; -.
DR EnsemblBacteria; AAP99589; AAP99589; Pro_0544.
DR GeneID; 54199911; -.
DR KEGG; pma:Pro_0544; -.
DR PATRIC; fig|167539.5.peg.559; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_2_0_3; -.
DR OMA; YVCDYYL; -.
DR OrthoDB; 729012at2; -.
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 Gene3D; 3.40.50.300; -; 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 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; Iron;
KW Iron-sulfur; Magnesium; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..296
FT /note="Light-independent protochlorophyllide reductase
FT iron-sulfur ATP-binding protein"
FT /id="PRO_0000324057"
FT BINDING 39..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT BINDING 209..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:2YNM"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:2YNM"
FT TURN 139..143
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:2YNM"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 258..274
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 286..292
FT /evidence="ECO:0007829|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
