A0A4D6JD75 · A0A4D6JD75_9MONI
- ProteinLight-independent protochlorophyllide reductase subunit N
- GenechlN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids466 (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
- 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 heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Pathway
Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 20 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner | ||||
Sequence: C | ||||||
Binding site | 45 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner | ||||
Sequence: C | ||||||
Binding site | 105 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner | ||||
Sequence: C |
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 subunit N
- EC number
- Short namesDPOR subunit N ; LI-POR subunit N
Gene names
Encoded on
- Chloroplast
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Polypodiopsida > Polypodiidae > Osmundales > Osmundaceae > Osmunda
Accessions
- Primary accessionA0A4D6JD75
Subcellular Location
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, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-421 | Nitrogenase/oxidoreductase component 1 | ||||
Sequence: CPISCVAWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIFAEPRYAMAELEEGDISAQLNDQEELKRLRLRIKRDRNPSVIIWIGTCTTEIIKMDLEGIAPKLETEPGVPIVVARANGLDYAFTQGEDTVLAAMTHRCPEHGSLGYKQKQDLVYGSDNPLVKPRRDDRKGKESENHPPLVLFGSLPSTVASQLNSELERQSIRVSGWLPSQRYAELPSLGEGVHVRGVNPFLSRTATTLMRRRKCRLIGAPFPIGPDGTRAWIEKICSVFGIKPHGLEERENLVWDNLKDYLRLVTGKSVFFTGDNLSEISLARFLIRCGMTVYEIGIPYMDKRYQAAELALLRNTCREMSIPMPRIVEKPDNYNQIQRMRELQPDLAITGMAHANPSEARGIDTKWSVEFTF | ||||||
Region | 173-195 | Disordered | ||||
Sequence: GSDNPLVKPRRDDRKGKESENHP | ||||||
Compositional bias | 178-193 | Basic and acidic residues | ||||
Sequence: LVKPRRDDRKGKESEN |
Sequence similarities
Belongs to the BchN/ChlN family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length466
- Mass (Da)52,810
- Last updated2019-07-03 v1
- Checksum9EB4807C583C3AF8
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 178-193 | Basic and acidic residues | ||||
Sequence: LVKPRRDDRKGKESEN |