ID A0A7H1KM38_PERAT Unreviewed; 352 AA. AC A0A7H1KM38; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 02-JUN-2021, entry version 3. 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:QNT28354.1}; OS Perovskia atriplicifolia (Russian sage) (Salvia yangii). OG Plastid; Chloroplast {ECO:0000313|EMBL:QNT28354.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salvia; OC Salvia subgen. Perovskia. OX NCBI_TaxID=268885 {ECO:0000313|EMBL:QNT28354.1}; RN [1] {ECO:0000313|EMBL:QPG24438.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=33193683; RA Gao C., Wu C., Zhang Q., Zhao X., Wu M., Chen R., Zhao Y., Li Z.; RT "Characterization of Chloroplast Genomes From Two Salvia Medicinal Plants RT and Gene Transfer Among Their Mitochondrial and Chloroplast Genomes."; RL Front. Genet. 11:0-574962(2020). RN [2] {ECO:0000313|EMBL:QNT28354.1} RP NUCLEOTIDE SEQUENCE. RA Zhao F., Drew B.T., Chen Y.-P., Hu G.-X., Li B., Xiang C.-L.; RT "The Chloroplast Genome of Salvia: Genomic Characterization and RT Phylogenetic Analysis."; RL Int. J. Plant Sci.:0-0(2020). RN [3] {ECO:0000313|EMBL:QQQ89480.1} RP NUCLEOTIDE SEQUENCE. RA Cao M.-T., Wu J.-J., Wang R.-H., Xu L., Qi Z.-C., Wei Y.-K.; RT "The complete chloroplast genome of Russian sage Salvia yangii B. T. Drew RT (Lamiaceae)."; RL Mitochondrial DNA B Resour 5:2590-2591(2020). RN [4] {ECO:0000313|EMBL:QPG24438.1} RP NUCLEOTIDE SEQUENCE. RA Gao C.-W., Li Z.-Q.; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:QQQ89480.1} RP NUCLEOTIDE SEQUENCE. RA Qi Z., Wu J., Cao M.; RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases. 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 membrane CC {ECO:0000256|ARBA:ARBA00004446}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004446}. Plastid, chloroplast thylakoid CC membrane {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 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; MN520025; QNT28354.1; -; Genomic_DNA. DR EMBL; MT012421; QPG24438.1; -; Genomic_DNA. DR EMBL; MT537168; QQQ89480.1; -; Genomic_DNA. DR SMR; A0A7H1KM38; -. 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:0042170; C:plastid 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:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC. 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 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:QNT28354.1}; 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:QNT28354.1}; 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_5029072323" FT PROPEP 345..352 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT /id="PRO_5029311395" 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 REGION 264..265 FT /note="Quinone (B)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 118 FT /note="Magnesium (chlorophyll-a ChlzD1 axial ligand); via FT tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 170 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 170 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 189 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 198 FT /note="Magnesium (chlorophyll-a PD1 axial ligand); via tele FT nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 215 FT /note="Iron; shared with heterodimeric partner; via tele FT nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 272 FT /note="Iron; shared with heterodimeric partner; via tele FT nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 332 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; FT via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 333 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 333 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 342 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 342 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 344 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via FT carboxylate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT METAL 344 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2; FT via carboxylate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 126 FT /note="Pheophytin D1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 215 FT /note="Quinone (B)" 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 352 AA; 38863 MW; 3FD660CAB4D6028D CRC64; MTAILERRES ESLWGRFCNW 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 LDLAAIEAPT NG //