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 27-MAR-2024, entry version 120. 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; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; pma:Pro_0544; -. DR PATRIC; fig|167539.5.peg.559; -. DR eggNOG; COG1348; Bacteria. DR HOGENOM; CLU_059373_2_0_3; -. DR OrthoDB; 9778641at2; -. 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 CDD; cd02032; Bchl-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01281; DPOR_bchL; 1. DR PANTHER; PTHR42864; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1. DR PANTHER; PTHR42864:SF2; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1. DR Pfam; PF00142; Fer4_NifH; 1. DR PIRSF; PIRSF000363; Nitrogenase_iron; 1. DR PRINTS; PR00091; NITROGNASEII. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 //