Detail Information for IndEnz0002009359
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