Detail Information for IndEnz0002011649
IED ID IndEnz0002011649
Enzyme Type ID protease011649
Protein Name Photosystem II protein D1 1
PSII D1 protein 1
EC 1.10.3.9
Photosystem II Q
B
protein 1
Gene Name psbA1 psbA-1 slr1181
Organism Synechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Merismopediaceae Synechocystis unclassified Synechocystis Synechocystis sp. PCC 6803 Synechocystis sp. (strain PCC 6803 / Kazusa)
Enzyme Sequence MTTTQLGLQEQSLWSRFCCWITSTSNRLYIGWFGVLMIPTLLTATTCFIIAFIAAPPVDIDGIREPIAGSLLYGNNIITAAVVPSSNAIGLHFYPIWEAHSLDEWLYNGGPYQLIVFHFLIGIFCYLGRQWELSYRLGMRPWICVAYSAPVAAATATLLIYSIGQGSFSDGLPLGISGTFNFMLVLQAEHNVLMHPFHMLGVAGVFGGALFAAMHGSLVTSSLIRETTEVESQNQGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRALHFFLGAWPVVGIWFAALAVCCFAFNLNGFNFNQSILDAQGRPVSTWADVINRANIGFEVMHERNVHNFPLDLASGDAQMVALNAPAIEG
Enzyme Length 360
Uniprot Accession Number P07826
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); Metal binding (14); Propeptide (1); Region (1); Sequence conflict (3); Site (3); Transmembrane (5)
Keywords Calcium;Chlorophyll;Chromophore;Electron transport;Herbicide resistance;Iron;Magnesium;Manganese;Membrane;Metal-binding;Oxidoreductase;Photosynthesis;Photosystem II;Reference proteome;Thylakoid;Transmembrane;Transmembrane helix;Transport
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305|PubMed:9512353}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305|PubMed:9512353}.
Modified Residue
Post Translational Modification PTM: C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305|PubMed:8034700}.; 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}.; PTM: C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 15328351; 18000013;
Motif
Gene Encoded By
Mass 39,651
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