Q8LU58 · CHLL_CHAGL
- ProteinLight-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
- GenechlL-A; chlL-B
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids290 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Component 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
- chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + 2 ATP + 2 H2O
CHEBI:83348 + RHEA-COMP:10004 CHEBI:33722 Position: 1CHEBI:33722 Position: 2+ 2 CHEBI:456216 + 2 CHEBI:43474 = CHEBI:83350 + RHEA-COMP:10002 CHEBI:33723 Position: 1CHEBI:33723 Position: 2+ 2 CHEBI:30616 + 2 CHEBI:15377
Cofactor
Note: Binds 1 [4Fe-4S] cluster per dimer.
Pathway
Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 10-15 | ATP (UniProtKB | ChEBI) | |||
Binding site | 14 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 39 | ATP (UniProtKB | ChEBI) | |||
Binding site | 95 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 129 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 180-181 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on iron-sulfur proteins as donors | |
Molecular Function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor | |
Biological Process | light-independent chlorophyll biosynthetic process | |
Biological Process | photosynthesis, dark reaction |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLight-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
- EC number
- Short namesDPOR subunit L ; LI-POR subunit L
Gene names
Encoded on
- Chloroplast
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Coleochaetophyceae > Coleochaetales > Chaetosphaeridiaceae > Chaetosphaeridium
Accessions
- Primary accessionQ8LU58
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000139552 | 1-290 | Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein | ||
Interaction
Subunit
Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB.
Structure
Sequence
- Sequence statusComplete
- Length290
- Mass (Da)31,794
- Last updated2002-10-01 v1
- MD5 Checksum9FE9844EBEC3090B66447C07CC98DFFF
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF494278 EMBL· GenBank· DDBJ | AAM96509.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF494278 EMBL· GenBank· DDBJ | AAM96591.1 EMBL· GenBank· DDBJ | Genomic DNA |