ID D1J7A6_ECTSI Unreviewed; 289 AA.
AC D1J7A6;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein {ECO:0000256|HAMAP-Rule:MF_00355};
DE Short=DPOR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
DE Short=LI-POR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
DE EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00355};
GN Name=chlL {ECO:0000313|EMBL:CAV31290.1};
GN ORFNames=Es_cpDNA_148 {ECO:0000313|EMBL:CAV31290.1}, Esil_142
GN {ECO:0000313|EMBL:QIE12488.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OG Plastid {ECO:0000313|EMBL:CAV31290.1}.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CAV31290.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAV31290.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=19835607; DOI=10.1186/1471-2148-9-253;
RA Le Corguille G., Pearson G., Valente M., Viegas C., Gschloessl B.,
RA Corre E., Bailly X., Peters A.F., Jubin C., Vacherie B., Cock J.M.,
RA Leblanc C.;
RT "Plastid genomes of two brown algae, Ectocarpus siliculosus and Fucus
RT vesiculosus: further insights on the evolution of red-algal derived
RT plastids.";
RL BMC Evol. Biol. 9:253-253(2009).
RN [3] {ECO:0000313|EMBL:QIE12488.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=32029782;
RA Choi J.W., Graf L., Peters A.F., Cock J.M., Nishitsuji K., Arimoto A.,
RA Shoguchi E., Nagasato C., Choi C.G., Yoon H.S.;
RT "Organelle inheritance and genome architecture variation in isogamous brown
RT algae.";
RL Sci. Rep. 10:0-2048(2020).
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:0000256|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:0000256|HAMAP-Rule:MF_00355};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00355};
CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000256|HAMAP-
CC Rule:MF_00355};
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC {ECO:0000256|ARBA:ARBA00005504, ECO:0000256|HAMAP-Rule:MF_00355,
CC ECO:0000256|RuleBase:RU003688}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00355}.
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DR EMBL; FP102343; CAT18837.1; -; Genomic_DNA.
DR EMBL; FP102296; CAV31290.1; -; Genomic_DNA.
DR EMBL; MN181444; QIE12488.1; -; Genomic_DNA.
DR RefSeq; YP_003289259.1; NC_013498.1.
DR AlphaFoldDB; D1J7A6; -.
DR STRING; 2880.D1J7A6; -.
DR GeneID; 8594880; -.
DR eggNOG; ENOG502QW4A; Eukaryota.
DR InParanoid; D1J7A6; -.
DR Proteomes; UP000002630; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
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 {ECO:0000256|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171, ECO:0000256|HAMAP-
KW Rule:MF_00355}; Chloroplast {ECO:0000313|EMBL:CAV31290.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00355};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00355};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00355};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_00355}; Plastid {ECO:0000313|EMBL:CAV31290.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00355"
FT BINDING 180..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00355"
SQ SEQUENCE 289 AA; 31624 MW; 8BAAAD933ED58388 CRC64;
MKLAVYGKGG IGKSTTSCNI SVALCRRGKR VLQIGCDPKH DSTFTLTGFL IPTIIDTLQA
KDYHYEDIWP EDVIYQGFGG VDCVEAGGPP AGAGCGGYVV GETVKLLKEL NAFDEYDVIL
FDVLGDVVCG GFAAPLNYAD YCLIVTDNGF DALFAANRIA ASVREKARTH ALRLAGLIGN
RTATRDLIDK YIDAVPMPVL EVLPLIEDIR VSRVKGKTLF EMTEFDSSLC YICDYYLNIA
DQLIANPEGV VPKEAADREL FSLLSDFYLN PTQKETENNV FEDAFDEIG
//
