AC   MF_00355;
DC   Protein; auto
TR   HAMAP; MF_00355; -; 1; level=0
XX
Names: ChlL_BchL
XX
case <OC:Bacteria> and not <OC:Cyanobacteriota>
ID   BCHL
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
ID   CHLL
end case
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;
case <OC:Bacteria> and not <OC:Cyanobacteriota>
GN   Name=bchL;
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
GN   Name=chlL;
end case
XX
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   -!- 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;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per dimer.;
end case
case <OC:Bacteria> and not <OC:Cyanobacteriota>
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC       biosynthesis (light-independent).
CC   -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of three
CC       subunits; BchL, BchN and BchB.
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
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.
end case
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
end case
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
XX
DR   Pfam; PF00142; Fer4_NifH; 1; trigger=no
DR   PIRSF; PIRSF000363; Nitrogenase_iron; 1; trigger=no
DR   PRINTS; PR00091; NITROGNASEII; 1; trigger=no
DR   NCBIfam; TIGR01281; DPOR_bchL; 1; trigger=no
DR   PROSITE; PS00746; NIFH_FRXC_1; 1; trigger=no
DR   PROSITE; PS00692; NIFH_FRXC_2; 1; trigger=no
DR   PROSITE; PS51026; NIFH_FRXC_3; 1; trigger=no
XX
KW   Oxidoreductase
KW   Photosynthesis
KW   Chlorophyll biosynthesis
case <OC:Bacteria> and not <OC:Cyanobacteriota>
KW   Bacteriochlorophyll biosynthesis
end case
KW   ATP-binding
KW   Nucleotide-binding
KW   Magnesium
KW   Metal-binding
case <FTGroup:1>
KW   Iron
KW   Iron-sulfur
KW   4Fe-4S
end case
XX
GO   GO:0005524; F:ATP binding
GO   GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
case <FTGroup:1>
GO   GO:0051539; F:4 iron, 4 sulfur cluster binding
end case
case <OC:Bacteria> and not <OC:Cyanobacteriota>
GO   GO:0030494; P:bacteriochlorophyll biosynthetic process
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
GO   GO:0015995; P:chlorophyll biosynthetic process
end case
GO   GO:0015979; P:photosynthesis
case <OG:Chloroplast>
GO   GO:0009507; C:chloroplast
end case
XX
FT   From: BCHL_CERS4 (Q9RFD6)
FT   BINDING         41..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-[IV]-G-K-S-T
FT   BINDING         211..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: N-R
FT   BINDING         235..237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: P-x-L
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: S
FT   BINDING         126
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Group: 1; Condition: C
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Group: 1; Condition: C
FT   BINDING         70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
XX
Size: 245-331;
Related: MF_00533;
Template: Q9RFD6; P0CY53; D5ANS3;
Scope:
 Bacteria
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: External expert: Yuichi Fujita, fujita@protein.osaka-u.ac.jp
XX
# Revision 1.48 2023/06/01
//