ID A0A1Y1CV60_DENMN Unreviewed; 368 AA. AC A0A1Y1CV60; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 12-OCT-2022, entry version 16. 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:BAX84154.1}; OS Dendrobium moniliforme (Orchid) (Epidendrum moniliforme). OG Plastid; Chloroplast {ECO:0000313|EMBL:BAX84154.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae; OC Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium. OX NCBI_TaxID=142614 {ECO:0000313|EMBL:BAX84154.1}; RN [1] {ECO:0000313|EMBL:BAX84154.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28515737; DOI=10.3389/fpls.2017.00715; RA Niu Z., Xue Q., Zhu S., Sun J., Liu W., Ding X.; RT "The Complete Plastome Sequences of Four Orchid Species: Insights into the RT Evolution of the Orchidaceae and the Utility of Plastomic Mutational RT Hotspots."; RL Front. Plant Sci. 8:715-715(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. {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-176 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; AB893950; BAX84154.1; -; 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:BAX84154.1}; 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:BAX84154.1}; 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 16 FT /note="Removed" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT CHAIN 17..359 FT /note="Photosystem II protein D1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT /id="PRO_5023395719" FT PROPEP 360..368 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT /id="PRO_5011014754" FT TRANSMEM 44..70 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 91..112 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 124..144 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 156..176 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 213..233 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 288..310 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 133 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 141 FT /ligand="pheophytin a" FT /ligand_id="ChEBI:CHEBI:136840" FT /ligand_label="D1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 185 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 204 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 213 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 230 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 230 FT /ligand="a quinone" FT /ligand_id="ChEBI:CHEBI:132124" FT /ligand_label="B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 279..280 FT /ligand="a quinone" FT /ligand_id="ChEBI:CHEBI:132124" FT /ligand_label="B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 287 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 347 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 348 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 357 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 359 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT SITE 176 FT /note="Tyrosine radical intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT SITE 205 FT /note="Stabilizes free radical intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT SITE 359..360 FT /note="Cleavage; by CtpA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT MOD_RES 17 FT /note="N-acetylthreonine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT MOD_RES 17 FT /note="Phosphothreonine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" SQ SEQUENCE 368 AA; 40538 MW; 77D8358DF8E4A625 CRC64; MCLGVLENGI NQDLTMTAIL ERRESTSLWG RFCNWITSTE NRLYIGWFGV LMIPTLLTAT SVFIIAFIAA PPVDIDGIRE PVSGSLLYGN NIISGAIIPT SAAIGLHFYP IWEAASVDEW LYNGGPYELI VLHFLLGVAC YMGREWELSF RLGMRPWIAV AYSAPVAAAT AVFLIYPIGQ GSFSDGMPLG ISGTFNFMIV FQAEHNILMH PFHMLGVAGV FGGSLFSAMH GSLVTSSLIR ETTENESANE GYRFGQEEET YNIVAAHGYF GRLIFQYASF NNSRSLHFFL AAWPVVGIWF TALGISTMAF NLNGFNFNQS VVDSQGRVIN TWADIINRAN LGMEVMHERN AHNFPLDLAS VEAPSING //