ID A0A2D1GS15_9MAGN Unreviewed; 353 AA. AC A0A2D1GS15; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 22-FEB-2023, entry version 16. DE RecName: Full=Photosystem II D2 protein {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004333}; DE Short=PSII D2 protein {ECO:0000256|HAMAP-Rule:MF_01383}; DE EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01383}; DE AltName: Full=Photosystem Q(A) protein {ECO:0000256|HAMAP-Rule:MF_01383}; GN Name=psbD {ECO:0000256|HAMAP-Rule:MF_01383, GN ECO:0000313|EMBL:ATN95759.1}; OS Taxillus sutchuenensis. OG Plastid; Chloroplast {ECO:0000313|EMBL:ATN95759.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Santalales; Loranthaceae; Lorantheae; Scurrulinae; Taxillus. OX NCBI_TaxID=227910 {ECO:0000313|EMBL:ATN95759.1}; RN [1] {ECO:0000313|EMBL:ATN95759.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=29026168; DOI=10.1038/s41598-017-13401-4; RA Li Y., Zhou J.G., Chen X.L., Cui Y.X., Xu Z.C., Li Y.H., Song J.Y., RA Duan B.Z., Yao H.; RT "Gene losses and partial deletion of small single-copy regions of the RT chloroplast genomes of two hemiparasitic Taxillus species."; RL Sci. Rep. 7:12834-12834(2017). CC -!- FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone CC oxidoreductase that uses light energy to abstract electrons from H(2)O, CC generating O(2) and a proton gradient subsequently used for ATP CC formation. It consists of a core antenna complex that captures photons, CC and an electron transfer chain that converts photonic excitation into a CC charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer CC binds P680, the primary electron donor of PSII as well as several CC subsequent electron acceptors. D2 is needed for assembly of a stable CC PSII complex. {ECO:0000256|HAMAP-Rule:MF_01383}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; CC Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, CC ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; CC Evidence={ECO:0000256|ARBA:ARBA00001833, ECO:0000256|HAMAP- CC Rule:MF_01383}; CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA, CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, CC PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen- CC evolving complex and a large number of cofactors. It forms dimeric CC complexes. {ECO:0000256|HAMAP-Rule:MF_01383}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01383}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01383}. CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2) CC are entirely coordinated by water. {ECO:0000256|HAMAP-Rule:MF_01383}. CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. CC {ECO:0000256|ARBA:ARBA00008204, ECO:0000256|HAMAP-Rule:MF_01383, CC ECO:0000256|RuleBase:RU004331}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KY996493; ATN95759.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2D1GS15; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW. DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule. DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC. DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro. DR CDD; cd09288; Photosystem-II_D2; 1. DR Gene3D; 1.20.85.10; Photosystem II protein D1-like; 1. DR HAMAP; MF_01383; PSII_PsbD_D2; 1. DR InterPro; IPR036854; Photo_II_D1/D2_sf. DR InterPro; IPR000484; Photo_RC_L/M. DR InterPro; IPR005868; PSII_PsbD/D2. DR PANTHER; PTHR33149:SF47; PHOTOSYSTEM II D2 PROTEIN; 1. DR PANTHER; PTHR33149; PHOTOSYSTEM II PROTEIN D1; 1. DR Pfam; PF00124; Photo_RC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR SUPFAM; SSF81483; Bacterial photosystem II reaction centre, L and M subunits; 1. DR TIGRFAMs; TIGR01152; psbD; 1. DR PROSITE; PS00244; REACTION_CENTER; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP- KW Rule:MF_01383}; Chloroplast {ECO:0000313|EMBL:ATN95759.1}; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP- KW Rule:MF_01383}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP- KW Rule:MF_01383}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01383}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01383}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01383}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01383}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01383}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_01383}; KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP- KW Rule:MF_01383}; Plastid {ECO:0000313|EMBL:ATN95759.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01383}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01383}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01383}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01383}. FT TRANSMEM 28..50 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 111..129 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 141..161 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 167..185 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 197..217 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 267..292 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 118 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="ChlzD2" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383" FT BINDING 130 FT /ligand="pheophytin a" FT /ligand_id="ChEBI:CHEBI:136840" FT /ligand_label="D2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383" FT BINDING 143 FT /ligand="pheophytin a" FT /ligand_id="ChEBI:CHEBI:136840" FT /ligand_label="D2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383" FT BINDING 198 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="PD2" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383" FT BINDING 215 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383" FT BINDING 215 FT /ligand="a plastoquinone" FT /ligand_id="ChEBI:CHEBI:17757" FT /ligand_label="Q(A)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383" FT BINDING 262 FT /ligand="a plastoquinone" FT /ligand_id="ChEBI:CHEBI:17757" FT /ligand_label="Q(A)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383" FT BINDING 269 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383" SQ SEQUENCE 353 AA; 39596 MW; 20917B2FBE46F18A CRC64; MTIALGKFTK DEKDLFDSMD DWLRRDRFVF VGWSGLLLFP CAYFALGGWF TGTTFITSWY THGLASSYLE GCNFLTAAVS TPANSLAHSL LLLWGPEAQG DFTRWCQLGG LWTFVALHGA FGLIGFMLRQ FELARSVQLR PYNAIAFSAP IAVFVSVFLI YPLGQSGWFF APSFGVAAIF RFILFFQGFH NWTLNPFHMM GVAGVLGAAL LCAIHGATVE NTLFEDGDGA NTFRAFNPTQ AEETYSMVTA NRFWSQIFGV AFSNKRWLHF FMLFVPVTGL WMSALGVVGL ALNLRAYDFV SQEIRAAEDP EFETFYTKNI LLNEGIRAWM ATQDQPHENL IFPEEVLPRG NAL //