Q32904 · CB23_PEA
- ProteinChlorophyll a-b binding protein 3, chloroplastic
- Genelhca3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids275 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.
Cofactor
Note: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 58 | Mg (UniProtKB | ChEBI) of chlorophyll b 1 (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 78 | chlorophyll a 1 (UniProtKB | ChEBI) | |||
Binding site | 84 | chlorophyll a 1 (UniProtKB | ChEBI) | |||
Binding site | 102 | Mg (UniProtKB | ChEBI) of chlorophyll a 1 (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 107 | chlorophyll b 2 (UniProtKB | ChEBI) | |||
Binding site | 142 | Mg (UniProtKB | ChEBI) of chlorophyll b 2 (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 169 | Mg (UniProtKB | ChEBI) of chlorophyll b 3 (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 172 | chlorophyll b 4 (UniProtKB | ChEBI) | |||
Binding site | 226 | chlorophyll a 5 (UniProtKB | ChEBI) | |||
Binding site | 227 | Mg (UniProtKB | ChEBI) of chlorophyll a 3 (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 230 | Mg (UniProtKB | ChEBI) of chlorophyll a 4 (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 232 | chlorophyll a 1 (UniProtKB | ChEBI) | |||
Binding site | 244 | Mg (UniProtKB | ChEBI) of chlorophyll a 5 (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 259 | Mg (UniProtKB | ChEBI) of chlorophyll a 6 (UniProtKB | ChEBI); axial binding residue | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast thylakoid membrane | |
Cellular Component | photosystem I | |
Cellular Component | photosystem II | |
Cellular Component | plastoglobule | |
Molecular Function | chlorophyll binding | |
Molecular Function | metal ion binding | |
Biological Process | photosynthesis, light harvesting in photosystem I | |
Biological Process | response to light stimulus |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameChlorophyll a-b binding protein 3, chloroplastic
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Fabeae > Pisum
Accessions
- Primary accessionQ32904
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Plastid, chloroplast thylakoid membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 233-253 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, transit peptide.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000310859 | ?-275 | Chlorophyll a-b binding protein 3, chloroplastic | ||
Transit peptide | 1-? | Chloroplast | |||
Post-translational modification
Photoregulated by reversible phosphorylation of its threonine residues.
Keywords
- PTM
Structure
Family & Domains
Domain
The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Sequence similarities
Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length275
- Mass (Da)29,607
- Last updated1996-11-01 v1
- Checksum49AB86D1CE247A31
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L19651 EMBL· GenBank· DDBJ | AAA84545.1 EMBL· GenBank· DDBJ | mRNA |