ID A0A5P8H9G6_9ASPA Unreviewed; 353 AA. AC A0A5P8H9G6; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 12-OCT-2022, entry version 8. DE RecName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004332}; DE Short=PSII D1 protein {ECO:0000256|HAMAP-Rule:MF_01379}; DE EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01379}; DE AltName: Full=Photosystem II Q(B) protein {ECO:0000256|HAMAP-Rule:MF_01379}; GN Name=psbA {ECO:0000256|HAMAP-Rule:MF_01379, GN ECO:0000313|EMBL:QFQ51717.1}; OS Spiranthes sinensis. OG Plastid; Chloroplast {ECO:0000313|EMBL:QFQ51717.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae; OC Orchidoideae; Cranichideae; Spiranthinae; Spiranthes. OX NCBI_TaxID=117406 {ECO:0000313|EMBL:QFQ51717.1}; RN [1] {ECO:0000313|EMBL:QFQ51717.1} RP NUCLEOTIDE SEQUENCE. RA Fan J., Huang M.-Y.; RT "Chloroplast genome structure and phylogeny of Spiranthes sinensis, an RT endangered medicinal orchid plant."; RL Mitochondrial DNA Part B Resour 4:2994-2996(2019). 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. {ECO:0000256|HAMAP-Rule:MF_01379}. 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|HAMAP-Rule:MF_01379}; CC -!- COFACTOR: CC Note=The D1/D2 heterodimer binds P680, chlorophylls that are the CC primary electron donor of PSII, and subsequent electron acceptors. It CC shares a non-heme iron and each subunit binds pheophytin, quinone, CC additional chlorophylls, carotenoids and lipids. D1 provides most of CC the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex CC (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is CC required for oxygen evolution. The PSII complex binds additional CC chlorophylls, carotenoids and specific lipids. {ECO:0000256|HAMAP- CC Rule:MF_01379}; 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_01379}. 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_01379}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- PTM: C-terminally processed by CtpA; processing is essential to allow CC assembly of the oxygen-evolving complex and thus photosynthetic growth. CC {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- PTM: Tyr-161 forms a radical intermediate that is referred to as redox- CC active TyrZ, YZ or Y-Z. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2) CC are entirely coordinated by water. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil bind CC in the Q(B) binding site and block subsequent electron transfer. CC {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. CC {ECO:0000256|ARBA:ARBA00008204, ECO:0000256|HAMAP-Rule:MF_01379, 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; MK936427; QFQ51717.1; -; 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:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; 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 GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW. DR CDD; cd09289; Photosystem-II_D1; 1. DR Gene3D; 1.20.85.10; -; 1. DR HAMAP; MF_01379; PSII_PsbA_D1; 1. DR InterPro; IPR036854; Photo_II_D1/D2_sf. DR InterPro; IPR000484; Photo_RC_L/M. DR InterPro; IPR005867; PSII_D1. DR PANTHER; PTHR33149; PTHR33149; 1. DR Pfam; PF00124; Photo_RC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR SUPFAM; SSF81483; SSF81483; 1. DR TIGRFAMs; TIGR01151; psbA; 1. DR PROSITE; PS00244; REACTION_CENTER; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|HAMAP-Rule:MF_01379}; KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP- KW Rule:MF_01379}; Chloroplast {ECO:0000313|EMBL:QFQ51717.1}; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP- KW Rule:MF_01379}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP- KW Rule:MF_01379}; KW Herbicide resistance {ECO:0000256|ARBA:ARBA00022646, ECO:0000256|HAMAP- KW Rule:MF_01379}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01379}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01379}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01379}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01379}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01379}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_01379}; KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP- KW Rule:MF_01379}; Plastid {ECO:0000313|EMBL:QFQ51717.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01379}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01379}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01379}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01379}. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT CHAIN 2..344 FT /note="Photosystem II protein D1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT /id="PRO_5024519990" FT PROPEP 345..353 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT /id="PRO_5024519989" FT TRANSMEM 29..55 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 76..97 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 109..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..186 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 198..218 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 273..295 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="ChlzD1" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 126 FT /ligand="pheophytin a" FT /ligand_id="ChEBI:CHEBI:136840" FT /ligand_label="D1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 170 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 189 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 198 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="PD1" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" 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_01379" FT BINDING 215 FT /ligand="a quinone" FT /ligand_id="ChEBI:CHEBI:132124" FT /ligand_label="B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 264..265 FT /ligand="a quinone" FT /ligand_id="ChEBI:CHEBI:132124" FT /ligand_label="B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 272 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_01379" FT BINDING 332 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 333 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 342 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 344 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT SITE 161 FT /note="Tyrosine radical intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT SITE 190 FT /note="Stabilizes free radical intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT SITE 344..345 FT /note="Cleavage; by CtpA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT MOD_RES 2 FT /note="N-acetylthreonine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT MOD_RES 2 FT /note="Phosphothreonine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" SQ SEQUENCE 353 AA; 38835 MW; B05B5EC3804E2521 CRC64; MTAILEKRES TSLWGRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAAAAVFLI YPIGQGSFSD GMPLGISGTF NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYRFG QEGETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLASVEVPS ING //