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HAMAP rule MF_00355

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General rule information [?]

Accession MF_00355
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 48)
Name ChlL_BchL
Scope(s) Bacteria
Plastid
Template(s) Q9RFD6 (BCHL_CERS4); P0CY53 (BCHL_RHOCA); D5ANS3 (BCHL_RHOCB); [ Recover all ]
Triggered by HAMAP; MF_00355 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Bacteria> and not <OC:Cyanobacteriota>
Identifier BCHL
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
Identifier CHLL
end case
Protein name RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein;
                 Short=DPOR subunit L;
                 Short=LI-POR subunit L;
                 EC=1.3.7.7;
case <OC:Bacteria> and not <OC:Cyanobacteriota>
Gene name Name=bchL;
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
Gene name Name=chlL;
end case

Comments [?]

FUNCTIONComponent of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
CATALYTIC ACTIVITY Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe- 4S]-[ferredoxin]; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:43474, ChEBI:CHEBI:83348, ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7;
case <FTGroup:1>
COFACTOR Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per dimer.;
end case
case <OC:Bacteria> and not <OC:Cyanobacteriota>
PATHWAYPorphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis (light-independent).
SUBUNITHomodimer. Protochlorophyllide reductase is composed of three subunits; BchL, BchN and BchB.
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
PATHWAYPorphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
SUBUNITHomodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB.
end case
case <OG:Chloroplast>
SUBCELLULAR LOCATIONPlastid, chloroplast.
end case
SIMILARITYBelongs to the NifH/BchL/ChlL family.

Keywords [?]


Gene Ontology [?]

GO:0005524; Molecular function:ATP binding
GO:0016636; Molecular function:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
case <FTGroup:1>
GO:0051539; Molecular function:4 iron, 4 sulfur cluster binding
end case
case <OCellular component:Bacteria> and not <OC:Cyanobacteriota>
GO:0030494; Biological process:bacteriochlorophyll biosynthetic process
end case
case <OCellular component:Cyanobacteriota> or <OG:Chloroplast>
GO:0015995; Biological process:chlorophyll biosynthetic process
end case
GO:0015979; Biological process:photosynthesis
case <OG:Chloroplast>
GO:0009507; Cellular component:chloroplast
end case

Cross-references [?]

Pfam PF00142; Fer4_NifH; 1;
PIRSF PIRSF000363; Nitrogenase_iron; 1;
PRINTS PR00091; NITROGNASEII; 1;
NCBIfam TIGR01281; DPOR_bchL; 1;
PROSITE PS00746; NIFH_FRXC_1; 1;
PROSITE PS00692; NIFH_FRXC_2; 1;
PROSITE PS51026; NIFH_FRXC_3; 1;

Features [?]

From: BCHL_CERS4 (Q9RFD6)
Key From To Description Tag Condition FTGroup
BINDING 41 46 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
G-[IV]-G-K-S-T
BINDING 211 212 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
N-R
BINDING 235 237 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
P-x-L
BINDING 45 45 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
S
BINDING 126 126 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_note="ligand shared between dimeric partners"
C 1
BINDING 160 160 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_note="ligand shared between dimeric partners"
C 1
BINDING 70 70 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
K

Additional information [?]

Size range 245-331 amino acids
Related rules MF_00533
Fusion Nter: None Cter: None
Comments External expert: Yuichi Fujita, fujita@protein.osaka-u.ac.jp



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