ID A0A2D1GS15_9MAGN Unreviewed; 353 AA. AC A0A2D1GS15; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 05-DEC-2018, entry version 5. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; Santalales; Loranthaceae; Lorantheae; Scurrulinae; OC Taxillus. OX NCBI_TaxID=227910 {ECO:0000313|EMBL:ATN95759.1}; RN [1] {ECO:0000313|EMBL:ATN95759.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=29026168; DOI=.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: CC plastoquinone oxidoreductase that uses light energy to abstract CC electrons from H(2)O, generating O(2) and a proton gradient CC subsequently used for ATP formation. It consists of a core antenna CC complex that captures photons, and an electron transfer chain that CC converts photonic excitation into a charge separation. The D1/D2 CC (PsbA/PsbA) reaction center heterodimer binds P680, the primary CC electron donor of PSII as well as several subsequent electron CC acceptors. D2 is needed for assembly of a stable PSII complex. CC {ECO:0000256|HAMAP-Rule:MF_01383}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + CC O2; Xref=Rhea:RHEA:36359, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192, CC Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562; EC=1.10.3.9; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01383}; CC -!- COFACTOR: CC Note=The D1/D2 heterodimer binds P680, chlorophylls that are the CC primary electron donor of PSII, and subsequent electron acceptors. CC It shares a non-heme iron and each subunit binds pheophytin, CC quinone, additional chlorophylls, carotenoids and lipids. There is CC also a Cl(-1) ion associated with D1 and D2, which is required for CC oxygen evolution. The PSII complex binds additional chlorophylls, CC carotenoids and specific lipids. {ECO:0000256|HAMAP- CC Rule:MF_01383}; CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins CC PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, CC PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral CC proteins of the oxygen-evolving complex and a large number of CC cofactors. It forms dimeric complexes. {ECO:0000256|HAMAP- CC Rule:MF_01383}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01383}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01383}. CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and CC ChlD2) are entirely coordinated by water. {ECO:0000256|HAMAP- CC Rule:MF_01383}. CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. CC {ECO:0000256|HAMAP-Rule:MF_01383, 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 GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro. DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. DR CDD; cd09288; Photosystem-II_D2; 1. DR Gene3D; 1.20.85.10; -; 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; PTHR33149; 1. DR Pfam; PF00124; Photo_RC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR SUPFAM; SSF81483; SSF81483; 1. DR TIGRFAMs; TIGR01152; psbD; 1. DR PROSITE; PS00244; REACTION_CENTER; 1. PE 3: Inferred from homology; KW Chlorophyll {ECO:0000256|HAMAP-Rule:MF_01383}; KW Chloroplast {ECO:0000313|EMBL:ATN95759.1}; KW Chromophore {ECO:0000256|HAMAP-Rule:MF_01383}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_01383, KW ECO:0000256|RuleBase:RU004333}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004333}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01383}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01383, KW ECO:0000256|RuleBase:RU004333, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01383, KW ECO:0000256|RuleBase:RU004333}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01383}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01383, KW ECO:0000256|RuleBase:RU004333}; KW Photosystem II {ECO:0000256|HAMAP-Rule:MF_01383, KW ECO:0000256|RuleBase:RU004333}; KW Plastid {ECO:0000313|EMBL:ATN95759.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01383}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01383, KW ECO:0000256|RuleBase:RU004333, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01383, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01383, KW ECO:0000256|RuleBase:RU004333}. FT TRANSMEM 28 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 185 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 197 217 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 267 292 Helical. {ECO:0000256|SAM:Phobius}. FT METAL 118 118 Magnesium (chlorophyll-a ChlzD2, axial FT ligand; peripheral); via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01383}. FT METAL 198 198 Magnesium (chlorophyll-a PD2 axial FT ligand); via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01383}. FT METAL 215 215 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01383}. FT METAL 269 269 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01383}. FT BINDING 130 130 Pheophytin D2. {ECO:0000256|HAMAP-Rule: FT MF_01383}. FT BINDING 143 143 Pheophytin D2. {ECO:0000256|HAMAP-Rule: FT MF_01383}. FT BINDING 215 215 Plastoquinone Q(A). {ECO:0000256|HAMAP- FT Rule:MF_01383}. FT BINDING 262 262 Plastoquinone Q(A); via amide nitrogen. FT {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 //