F4XXR7 · F4XXR7_9CYAN
- ProteinLight-independent protochlorophyllide reductase subunit B
- GenechlB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids508 (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 NB-protein (ChlN-ChlB) is the catalytic component of the complex.
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 heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Pathway
Porphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis.
Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 36 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner | |||
Active site | 294 | Proton donor | |||
Binding site | 429-430 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
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 | bacteriochlorophyll biosynthetic process | |
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 subunit B
- EC number
- Short namesDPOR subunit B ; LI-POR subunit B
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Oscillatoriales > Oscillatoriaceae > Moorena
Accessions
- Primary accessionF4XXR7
Proteomes
Interaction
Subunit
Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 12-426 | Nitrogenase/oxidoreductase component 1 | |||
Domain | 459-503 | Light-independent protochlorophyllide reductase subunit B-like C-terminal | |||
Sequence similarities
Belongs to the ChlB/BchB/BchZ family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length508
- Mass (Da)56,921
- Last updated2011-06-28 v1
- MD5 Checksum689E64CBE93B77E3D05B72BFDDF29A53
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL890949 EMBL· GenBank· DDBJ | EGJ30628.1 EMBL· GenBank· DDBJ | Genomic DNA |