R4ZGW2 · R4ZGW2_PICAB
- ProteinLight-independent protochlorophyllide reductase subunit N
- GenechlN
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids468 (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; chlorophyll biosynthesis (light-independent).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 22 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner | ||||
Sequence: C | ||||||
Binding site | 47 | [4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner | ||||
Sequence: C | ||||||
Binding site | 107 | [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
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Pinopsida > Pinidae > Conifers I > Pinales > Pinaceae > Picea
Accessions
- Primary accessionR4ZGW2
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-439 | Nitrogenase/oxidoreductase component 1 | ||||
Sequence: CPISCVSWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIFAEPRYAMAELEEGDISAHLNDYEELKTLCIRIRKDRDPSVIIWIGTCTTEIIKMDLEGMAPKLEYEIGIPILVARANGLDYAFTQGEDTVLAVMAHRCPEQEFPIGESKETITKTKLFPFPLLKEKKLVEYANHPPLVIFGSLPSNLVSQLDTELRRQFIKVSGWLPAQRYADLPSLGDGVYVCGVNPFLGRTATTLIRRKKCELIVAPFPIGPDGTRAWIERICPVFGIETQSLEEREERIWESLKDYLDLVRGKSVFFMGDNLLEISLARFLIRCGMIVYEIGIPYMDKRYQAAELALLKDTCIKMCIPIPRIVEKPDNSNQIRRMRELQPDLAITGMAHANPLGARGIDTKWSVEFTFAQIHGFASARDVLELVTR |
Sequence similarities
Belongs to the BchN/ChlN family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length468
- Mass (Da)53,286
- Last updated2013-07-24 v1
- Checksum5DD24F5793E68E23
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HF937082 EMBL· GenBank· DDBJ | CCW23147.1 EMBL· GenBank· DDBJ | Genomic DNA |