ID CHLL_CYAPA Reviewed; 282 AA. AC P48110; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 02-SEP-2026, entry version 128. 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}; Synonyms=frxC; OS Cyanophora paradoxa. OG Plastid; Cyanelle. OC Eukaryota; Glaucocystophyceae; Cyanophorales; Cyanophoraceae; Cyanophora. OX NCBI_TaxID=2762; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UTEX LB 555 / Pringsheim; RX DOI=10.1007/BF02669186; RA Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J., RA Bryant D.A.; RT "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa."; RL Plant Mol. Biol. Rep. 13:327-332(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UTEX LB 555 / Pringsheim; RX DOI=10.1007/978-3-642-60885-8_3; RA Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M., RA Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M., RA Jakowitsch J., Bohnert H.J., Bryant D.A.; RT "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the RT genetic complexity of a primitive plastid."; RL (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W. RL (eds.); RL Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997). 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=chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 CC phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + CC 2 ATP + 2 H2O; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002, Rhea:RHEA- CC COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33722, CC ChEBI:CHEBI:33723, ChEBI:CHEBI:43474, ChEBI:CHEBI:83348, CC 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 -!- SUBCELLULAR LOCATION: Plastid, cyanelle. 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; U30821; AAA81316.1; -; Genomic_DNA. DR PIR; T06973; T06973. DR RefSeq; NP_043285.1; NC_001675.1. DR AlphaFoldDB; P48110; -. DR SMR; P48110; -. DR GeneID; 801629; -. DR UniPathway; UPA00670; -. DR GO; GO:0009842; C:cyanelle; IEA:UniProtKB-SubCell. 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: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 3: Inferred from homology; KW 4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis; KW Chlorophyll biosynthesis; Cyanelle; Iron; Iron-sulfur; Magnesium; KW Metal-binding; Nucleotide-binding; Oxidoreductase; Photosynthesis; Plastid. FT CHAIN 1..282 FT /note="Light-independent protochlorophyllide reductase FT iron-sulfur ATP-binding protein" FT /id="PRO_0000139556" FT BINDING 10..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355" FT BINDING 14 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355" FT BINDING 95 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 129 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 180..181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00355" SQ SEQUENCE 282 AA; 30847 MW; BC5072D21AE28684 CRC64; MKLAVYGKGG IGKSTTSCNI SVALAKRGKK VLQIGCDPKH DSTFTLTGHL IPTIIDTLQE KDFHYEDIWP EDVIYKGYAG VDCVEAGGPP AGAGCGGYVV GETVKLLKEL NAFDEYDIIL FDVLGDVVCG GFASPLNYAD YCLIVTDNGF DALFAANRIA ASVREKARTH QLRLAGLIGN RTTKSDLIEK YTENVPIPIL QLLPLIEDIR ISRVKGKTLF EMSESNPELS PICDYYLNIA DQILAKPEGI IPNEVLDRDL FTLLSDFYLN MDSSESSNLT LV //