K9UMX2 · K9UMX2_CHAP6
- ProteinPhotosystem II protein D1
- GenepsbA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids424 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Miscellaneous
2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water.
Cyanobacteriota usually contain more than 2 copies of the psbA gene.
Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer.
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, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 182 | Mg (UniProtKB | ChEBI) of chlorophyll a ChlzD1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 190 | pheophytin a D1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Site | 225 | Tyrosine radical intermediate | ||||
Sequence: Y | ||||||
Binding site | 234 | [CaMn4O5] cluster (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 253 | [CaMn4O5] cluster (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 254 | Stabilizes free radical intermediate | ||||
Sequence: H | ||||||
Binding site | 262 | Mg (UniProtKB | ChEBI) of chlorophyll a PD1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 279 | Fe cation (UniProtKB | ChEBI); ligand shared with heterodimeric partner | ||||
Sequence: H | ||||||
Binding site | 279 | a quinone B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 328-329 | a quinone B (UniProtKB | ChEBI) | ||||
Sequence: SF | ||||||
Binding site | 336 | Fe cation (UniProtKB | ChEBI); ligand shared with heterodimeric partner | ||||
Sequence: H | ||||||
Binding site | 396 | [CaMn4O5] cluster (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 397 | [CaMn4O5] cluster (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 406 | [CaMn4O5] cluster (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 408 | [CaMn4O5] cluster (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Site | 408-409 | Cleavage; by CtpA | ||||
Sequence: AA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | photosystem II | |
Cellular Component | plasma membrane-derived thylakoid membrane | |
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, acting on diphenols and related substances as donors, oxygen as acceptor | |
Molecular Function | oxygen evolving activity | |
Biological Process | photosynthetic electron transport in photosystem II | |
Biological Process | response to herbicide |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhotosystem II protein D1
- EC number
- Short namesPSII D1 protein
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Gomontiellales > Chamaesiphonaceae > Chamaesiphon
Accessions
- Primary accessionK9UMX2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cellular thylakoid membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 93-119 | Helical | ||||
Sequence: YVGWFGVLMVPTLLSATICFIIAFIAA | ||||||
Transmembrane | 175-193 | Helical | ||||
Sequence: PYQLVVFHFLIGIFCYMGR | ||||||
Transmembrane | 205-225 | Helical | ||||
Sequence: PWICVAYSAPVAAATAVFLIY | ||||||
Transmembrane | 262-282 | Helical | ||||
Sequence: HMLGVAGVFGGSLFSAMHGSL | ||||||
Transmembrane | 337-359 | Helical | ||||
Sequence: FFLGAWPVVGIWFTSLGVSTMAF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5023376532 | 1-408 | Photosystem II protein D1 | |||
Sequence: MSPEIQLSSLCVQKMTRSPVITKPDDSHKVYKPEKGLQTLTIELNYVHTSKTFRSTRNTSNHKTMTTTLQRTQNANVWDRFCSWITSTENRIYVGWFGVLMVPTLLSATICFIIAFIAAPPVDIDGIREPVAGSLMFGNNIISGAVIPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVVFHFLIGIFCYMGREWELSYRLGMRPWICVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTEVESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGAWPVVGIWFTSLGVSTMAFNLNGFNFNQSVVDSQGRGINTWADIINRANLGMEVMHERNAHNFPLDLA | ||||||
Propeptide | PRO_5007347382 | 409-424 | ||||
Sequence: AGEATPVALTAPAING |
Post-translational modification
C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth.
Tyr-225 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
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, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length424
- Mass (Da)46,973
- Last updated2013-03-06 v1
- Checksum9DF4A1549BD3BB9C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003600 EMBL· GenBank· DDBJ | AFY96170.1 EMBL· GenBank· DDBJ | Genomic DNA |