Q85FN8 · CHLB_ADICA
- ProteinLight-independent protochlorophyllide reductase subunit B
- GenechlB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids518 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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, active site.
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 B
- EC number
- Short namesDPOR subunit B ; LI-POR subunit B
Gene names
Encoded on
- Chloroplast
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Polypodiopsida > Polypodiidae > Polypodiales > Pteridineae > Pteridaceae > Vittarioideae > Adiantum
Accessions
- Primary accessionQ85FN8
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000219808 | 1-518 | Light-independent protochlorophyllide reductase subunit B | |||
Sequence: MKLAYWMYAGPAHIGTLRVASSFRNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASVVDRHVLARGSRDKVVSNISRKGEEQRPDLIVLTPTCTSSILQEDLQNFVDRASLYSESDVILADVNHYRVNELQASDKTLEQIVRYYLDRARKEGIFNRSLTDVPSANIIGILTLGFHNQHDCRELKRLLGELGVSINQIIPEGEFLNNLKDLPRAWFNIVPYREIGLMAASFLEKEYGMPYISTTPIGISNTADFVMQVEKLMNFWATVLLGKKFHYDQYVENQTKFVSQAAWFSKSIDCQNLAGKEAVVFGDATHAASITKILSGEMGIRVSCSGTYCKHDAGWFNEQVQGLCDEVIITEDHTEVGDTIARIEPSAIFGTQMERHIGKRIDIPCGVISSPVHIQNFPLGYRPFMGYEGTNQISDLIYNSFNLGMEDHLLDVFGGHDTKGISTKSLSTGGKSIDWTPEAESELKRIPGFVRGKVKKNTEVFARQNNILKITVDVMYAAKERRSIESLA |
Interaction
Subunit
Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits.
Structure
Sequence
- Sequence statusComplete
- Length518
- Mass (Da)58,221
- Last updated2004-08-16 v2
- ChecksumADC05513672FE61C
RNA Editing
Edited at positions 5 6 46 84 189 192 275 311 345 409 439 440 473
The nonsense codon at position 84 is modified to a sense codon
Keywords
- Coding sequence diversity
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY178864 EMBL· GenBank· DDBJ | AAP29373.2 EMBL· GenBank· DDBJ | Genomic DNA |