A0A386B0J3 · A0A386B0J3_CODAR
- ProteinLight-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
- GenechlL
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids285 (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
- 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
2 CHEBI:456216 + CHEBI:83348 + RHEA-COMP:10004 CHEBI:33722 Position: 1CHEBI:33722 Position: 2+ 2 CHEBI:43474 = 2 CHEBI:30616 + 2 CHEBI:15377 + CHEBI:83350 + RHEA-COMP:10002 CHEBI:33723 Position: 1CHEBI:33723 Position: 2
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) | ||||
Sequence: GIGKST | ||||||
Binding site | 14 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 39 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 95 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 129 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 180-181 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NR |
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
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Chlorophyta > Ulvophyceae > TCBD clade > Bryopsidales > Bryopsidineae > Codiaceae > Codium
Accessions
- Primary accessionA0A386B0J3
Subcellular Location
Interaction
Subunit
Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB.
Structure
Sequence
- Sequence statusComplete
- Length285
- Mass (Da)31,618
- Last updated2018-12-05 v1
- ChecksumE5576B09B74D30FC