ID A0A1Y1CV60_DENMN Unreviewed; 368 AA. AC A0A1Y1CV60; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 10-APR-2019, entry version 9. 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; Magnoliophyta; 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 RT the Evolution of the Orchidaceae and the Utility of Plastomic RT Mutational Hotspots."; RL Front. Plant Sci. 8:715-715(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. {ECO:0000256|HAMAP-Rule:MF_01379}. 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_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. CC It shares a non-heme iron and each subunit binds pheophytin, CC quinone, additional chlorophylls, carotenoids and lipids. D1 CC provides most of the ligands for the Mn4-Ca-O5 cluster of the CC oxygen-evolving complex (OEC). There is also a Cl(-1) ion CC associated with D1 and D2, which is required for oxygen evolution. CC The PSII complex binds additional chlorophylls, carotenoids and CC specific lipids. {ECO:0000256|HAMAP-Rule:MF_01379}; 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_01379}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01379}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- PTM: C-terminally processed by CtpA; processing is essential to CC allow assembly of the oxygen-evolving complex and thus CC photosynthetic growth. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- PTM: Tyr-176 forms a radical intermediate that is referred to as CC redox-active TyrZ, YZ or Y-Z. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and CC ChlD2) are entirely coordinated by water. {ECO:0000256|HAMAP- CC Rule:MF_01379}. CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil CC bind in the Q(B) binding site and block subsequent electron CC transfer. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. CC {ECO:0000256|HAMAP-Rule:MF_01379, 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:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro. DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 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 Calcium {ECO:0000256|HAMAP-Rule:MF_01379}; KW Chlorophyll {ECO:0000256|HAMAP-Rule:MF_01379}; KW Chloroplast {ECO:0000313|EMBL:BAX84154.1}; KW Chromophore {ECO:0000256|HAMAP-Rule:MF_01379}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Herbicide resistance {ECO:0000256|HAMAP-Rule:MF_01379}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004332}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01379}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01379}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Photosystem II {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Plastid {ECO:0000313|EMBL:BAX84154.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01379}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}. FT INIT_MET 16 16 Removed. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT PROPEP 360 368 {ECO:0000256|HAMAP-Rule:MF_01379}. FT /FTId=PRO_5011014754. FT TRANSMEM 44 70 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 124 144 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 156 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 213 233 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 288 310 Helical. {ECO:0000256|SAM:Phobius}. FT REGION 279 280 Quinone (B). {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 133 133 Magnesium (chlorophyll-a ChlzD1 axial FT ligand); via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 185 185 Calcium-manganese-oxide [Ca-4Mn-5O]; FT calcium. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 185 185 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 4. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 204 204 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 213 213 Magnesium (chlorophyll-a PD1 axial FT ligand); via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 230 230 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 287 287 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 347 347 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 348 348 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 3. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 348 348 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 4. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 357 357 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 357 357 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 359 359 Calcium-manganese-oxide [Ca-4Mn-5O]; FT calcium; via carboxylate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 359 359 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2; via carboxylate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT BINDING 141 141 Pheophytin D1. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT BINDING 230 230 Quinone (B). {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT SITE 176 176 Tyrosine radical intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT SITE 205 205 Stabilizes free radical intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT SITE 359 360 Cleavage; by CtpA. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT MOD_RES 17 17 N-acetylthreonine. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT MOD_RES 17 17 Phosphothreonine. {ECO:0000256|HAMAP- FT 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 //