A0A8E4BZM8 · A0A8E4BZM8_9CHLO
- ProteinPhotosystem II D2 protein
- GenepsbD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids352 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H2O, generating O2 and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
Miscellaneous
2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water.
Catalytic activity
- 2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2
2 a plastoquinone RHEA-COMP:9562 + 2 CHEBI:15377 + 4 CHEBI:30212 = 2 a plastoquinol RHEA-COMP:9561 + CHEBI:15379
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 117 | Mg (UniProtKB | ChEBI) of chlorophyll a ChlzD2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 129 | pheophytin a D2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 142 | pheophytin a D2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 197 | Mg (UniProtKB | ChEBI) of chlorophyll a PD2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 214 | Fe cation (UniProtKB | ChEBI); ligand shared with heterodimeric partner | ||||
Sequence: H | ||||||
Binding site | 214 | a plastoquinone Q(A) (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 261 | a plastoquinone Q(A) (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 268 | Fe cation (UniProtKB | ChEBI); ligand shared with heterodimeric partner | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast thylakoid membrane | |
Cellular Component | photosystem II | |
Molecular Function | chlorophyll binding | |
Molecular Function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity | |
Molecular Function | iron ion binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | photosynthetic electron transport in photosystem II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhotosystem II D2 protein
- EC number
- Short namesPSII D2 protein
- Alternative names
Gene names
Encoded on
- Chloroplast
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Chlorophyta > core chlorophytes > Trebouxiophyceae > Trebouxiophyceae incertae sedis > Coccomyxaceae > Medakamo
Accessions
- Primary accessionA0A8E4BZM8
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Plastid, chloroplast thylakoid membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 27-49 | Helical | ||||
Sequence: FVFVGWSGLLLLPNAYFALGGWF | ||||||
Transmembrane | 110-128 | Helical | ||||
Sequence: LWTFVALHGAFALIGFMLR | ||||||
Transmembrane | 140-160 | Helical | ||||
Sequence: PYNAIAFSAPIAVFVSVFLIY | ||||||
Transmembrane | 166-184 | Helical | ||||
Sequence: GWFFAPSFGVAAIFRFILF | ||||||
Transmembrane | 196-216 | Helical | ||||
Sequence: FHMMGVAGVLGAALLCAIHGA | ||||||
Transmembrane | 266-291 | Helical | ||||
Sequence: WLHFFMLFVPVTGLWMSAIGVVGLAL |
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
Structure
Sequence
- Sequence statusComplete
- Length352
- Mass (Da)39,505
- Last updated2022-01-19 v1
- Checksum22BE4E6B78F10832