ID   CHLL_POLAC              Reviewed;         160 AA.
AC   P36439;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein;
DE            Short=DPOR subunit L;
DE            Short=LI-POR subunit L;
DE            EC=1.3.7.7;
DE   Flags: Fragment;
GN   Name=chlL; Synonyms=frxC;
OS   Polystichum acrostichoides (Christmas fern) (Nephrodium acrostichoides).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Polypodiineae; Dryopteridaceae;
OC   Dryopteridoideae; Polystichum.
OX   NCBI_TaxID=28470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RX   AGRICOLA=IND20364704; DOI=10.1007/BF00994092;
RA   Burke D.H., Raubeson L.A., Alberti M., Hearst J.E., Jordan E.T.,
RA   Kirch S.A., Valinski A.E.C., Conant D.S., Stein D.B.;
RT   "The chlL (frxC) gene: phylogenetic distribution in vascular plants and DNA
RT   sequence from Polystichum acrostichoides (Pteridophyta) and Synechococcus
RT   sp. 7002 (Cyanobacteria).";
RL   Plant Syst. Evol. 187:89-102(1993).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis (light-independent).
CC   -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of three
CC       subunits; ChlL, ChlN and ChlB (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
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DR   EMBL; U00732; AAA67136.1; -; Genomic_DNA.
DR   AlphaFoldDB; P36439; -.
DR   SMR; P36439; -.
DR   UniPathway; UPA00670; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030655; NifH/chlL_CS.
DR   InterPro; IPR000392; NifH/frxC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42864; PTHR42864; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   SUPFAM; SSF52540; SSF52540; 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; Chlorophyll biosynthesis; Chloroplast; Iron;
KW   Iron-sulfur; Magnesium; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW   Photosynthesis; Plastid.
FT   CHAIN           1..>160
FT                   /note="Light-independent protochlorophyllide reductase
FT                   iron-sulfur ATP-binding protein"
FT                   /id="PRO_0000139567"
FT   BINDING         15..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   NON_TER         160
SQ   SEQUENCE   160 AA;  17083 MW;  ED401E851D3FE56B CRC64;
     MELRETKVAV YGKGGIGKST TSCNTSIALA RRGRRILQIG CDPKHDSTFT PTGFSIPTII
     DTSQSKDYHY EDVWPEDVIH RGYGGVDCVE AGGPPAGAGC GGYVVGETVK PLKESNAFYE
     YDIILFDVLG DVVCGGFAAP LNYADYCIII TDNGFDALSA