ID A0A3G2Z2Z4_9LILI Unreviewed; 353 AA. AC A0A3G2Z2Z4; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 31-JUL-2019, entry version 6. 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:AYP33695.1}; OS Heliconia meridensis. OG Plastid {ECO:0000313|EMBL:AYP33695.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Heliconiaceae; OC Heliconia. OX NCBI_TaxID=1932260 {ECO:0000313|EMBL:AYP33695.1}; RN [1] {ECO:0000313|EMBL:AYP33695.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=13772 {ECO:0000313|EMBL:AYP33695.1}; RX PubMed=30368769; DOI=.1002/ajb2.1178; RA Givnish T.J., Zuluaga A., Spalink D., Soto Gomez M., Lam V.K., RA Saarela J.M., Sass C., Iles W.J., de Sousa D.J., Leebens-Mack J., RA Chris Pires J., Zomlefer W.B., Gandolfo M.A., Davis J.I., RA Stevenson D.W., dePamphilis C., Specht C.D., Graham S.W., RA Barrett C.F., Ane C.; RT "Monocot plastid phylogenomics, timeline, net rates of species RT diversification, the power of multi-gene analyses, and a functional RT model for the origin of monocots."; RL Am. J. Bot. 105:1888-1910(2018). CC -!- FUNCTION: Photosystem II (PSII) is a light-driven CC water:plastoquinone oxidoreductase that uses light energy to CC abstract electrons from H(2)O, generating O(2) and a proton CC gradient subsequently used for ATP formation. It consists of a CC core antenna complex that captures photons, and an electron CC transfer chain that converts photonic excitation into a charge CC 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 CC stable PSII complex. {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, Rhea:RHEA-COMP:9561, Rhea:RHEA- CC COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; CC EC=1.10.3.9; 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: Cellular 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; MH603426; AYP33695.1; -; Genomic_DNA. 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:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell. 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 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:AYP33695.1}; 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; 39529 MW; AAABC041C9E3D2A8 CRC64; MTIAIGKITK EENDLFDIMD DWLRRDRFVF VGWSGLLLFP CAYFALGGWF TGTTFVTSWY THGLASSYLE GCNFLTAAVS TPANSLAHSL LLLWGPEAQG DFTRWCQLGG LWTFVALHGA FGLIGFMLRQ FELARSVQLR PYNAIAFSAP IAVFVSVFLI YPLGQSGWFF APSFGVAAIF RFILFFQGFH NWTLNPFHMM GVAGVLGAAL LCAIHGATVE NTLFEDGDGA NTFRAFNPTQ AEETYSMVTA NRFWSQIFGV AFSNKRWLHF FMLFVPVTGL WMSAIGVVGL ALNLRAYDFV SQEIRAAEDP EFETFYTKNI LLNEGIRAWM AAQDQPHENL VFPEEVLPRG NAL //