ID A0A481XPL6_9ASPA Unreviewed; 353 AA. AC A0A481XPL6; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 18-SEP-2019, entry version 4. 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:QBK39983.1}; OS Holcoglossum flavescens. OG Plastid {ECO:0000313|EMBL:QBK39983.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae; OC Epidendroideae; Vandeae; Aeridinae; Holcoglossum. OX NCBI_TaxID=536148 {ECO:0000313|EMBL:QBK39983.1}; RN [1] {ECO:0000313|EMBL:QBK39983.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30808310; DOI=.1186/s12862-019-1384-5; RA Li Z.H., Ma X., Wang D.Y., Li Y.X., Wang C.W., Jin X.H.; RT "Evolution of plastid genomes of Holcoglossum (Orchidaceae) with RT recent radiation."; RL BMC Evol. Biol. 19:63-63(2019). 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. {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: Cellular 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-161 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; MK442925; QBK39983.1; -; Genomic_DNA. DR EMBL; MK442926; QBK40057.1; -; Genomic_DNA. DR SMR; A0A481XPL6; -. 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: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 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:QBK39983.1}; 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 1 1 Removed. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT PROPEP 345 353 {ECO:0000256|HAMAP-Rule:MF_01379}. FT /FTId=PRO_5019872471. FT TRANSMEM 29 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 76 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 186 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 198 218 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 273 295 Helical. {ECO:0000256|SAM:Phobius}. FT REGION 264 265 Quinone (B). {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 118 118 Magnesium (chlorophyll-a ChlzD1 axial FT ligand); via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O]; FT calcium. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 4. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 189 189 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 198 198 Magnesium (chlorophyll-a PD1 axial FT ligand); via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 215 215 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 272 272 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 332 332 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 3. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 4. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O]; FT calcium; via carboxylate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2; via carboxylate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT BINDING 126 126 Pheophytin D1. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT BINDING 215 215 Quinone (B). {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT SITE 161 161 Tyrosine radical intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT SITE 190 190 Stabilizes free radical intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT SITE 344 345 Cleavage; by CtpA. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT MOD_RES 2 2 N-acetylthreonine. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT MOD_RES 2 2 Phosphothreonine. {ECO:0000256|HAMAP- FT Rule:MF_01379}. SQ SEQUENCE 353 AA; 38937 MW; 9EA8FC3531FA61DA CRC64; MTAILERRES TSLWGRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYRFG QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLASVEAPS ING //