IED ID | IndEnz0002009359 |
Enzyme Type ID | protease009359 |
Protein Name |
Photosystem II protein D1 PSII D1 protein EC 1.10.3.9 Photosystem II Q B protein |
Gene Name | psbA |
Organism | Tetradesmus obliquus (Green alga) (Acutodesmus obliquus) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Chlorophyta core chlorophytes Chlorophyceae CS clade Sphaeropleales Scenedesmaceae Tetradesmus Tetradesmus obliquus (Green alga) (Acutodesmus obliquus) |
Enzyme Sequence | MTAILAKNEASSLWARFCEWITSTENRLYIGWFGVIMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAVVPTSNAIGLHFYPIWEAASLDEWLYNGGPYQLIVCHFFLGICCYMGREWELSYRLGMRPWIAVAYSAPVAAATAVFIIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVLNTWADIINRANLGMEVMHERNAHNFPLDLASVEAPSVNA |
Enzyme Length | 353 |
Uniprot Accession Number | Q1KVU8 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 126; /note=Pheophytin D1; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; BINDING 215; /note=Quinone (B); /evidence=ECO:0000255|HAMAP-Rule:MF_01379 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01379}; |
DNA Binding | |
EC Number | 1.10.3.9 |
Enzyme Function | FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) 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/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. {ECO:0000255|HAMAP-Rule:MF_01379}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Binding site (2); Chain (1); Initiator methionine (1); Metal binding (14); Modified residue (2); Propeptide (1); Region (1); Site (3); Transmembrane (5) |
Keywords | Acetylation;Calcium;Chlorophyll;Chloroplast;Chromophore;Electron transport;Herbicide resistance;Iron;Magnesium;Manganese;Membrane;Metal-binding;Oxidoreductase;Phosphoprotein;Photosynthesis;Photosystem II;Plastid;Thylakoid;Transmembrane;Transmembrane helix;Transport |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}. |
Modified Residue | MOD_RES 2; /note=N-acetylthreonine; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; MOD_RES 2; /note=Phosphothreonine; /evidence=ECO:0000255|HAMAP-Rule:MF_01379 |
Post Translational Modification | PTM: The 9 C-terminal residues are removed, probably by CTPA (AC O04073); processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:9252339}.; PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | Chloroplast |
Mass | 38,894 |
Kinetics | |
Metal Binding | METAL 118; /note=Magnesium (chlorophyll-a ChlzD1 axial ligand); via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 170; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 170; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 189; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 198; /note=Magnesium (chlorophyll-a PD1 axial ligand); via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 215; /note=Iron; shared with heterodimeric partner; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 272; /note=Iron; shared with heterodimeric partner; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 332; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 333; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 333; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 342; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 342; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 344; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via carboxylate; /evidence=ECO:0000255|HAMAP-Rule:MF_01379; METAL 344; /note=Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2; via carboxylate; /evidence=ECO:0000255|HAMAP-Rule:MF_01379 |
Rhea ID | RHEA:36359 |
Cross Reference Brenda |