ID PSBA_ANTSP Reviewed; 360 AA. AC P24625; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 25-MAY-2022, entry version 113. DE RecName: Full=Photosystem II protein D1 {ECO:0000255|HAMAP-Rule:MF_01379}; DE Short=PSII D1 protein {ECO:0000255|HAMAP-Rule:MF_01379}; DE EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379}; DE AltName: Full=Photosystem II Q(B) protein {ECO:0000255|HAMAP-Rule:MF_01379}; DE Flags: Precursor; GN Name=psbA {ECO:0000255|HAMAP-Rule:MF_01379}; OS Antithamnion sp. (Red alga). OG Plastid; Chloroplast. OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales; OC Ceramiaceae; Antithamnion; unclassified Antithamnion. OX NCBI_TaxID=2767; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LB 95.79; RX PubMed=1934114; DOI=10.1007/bf00312783; RA Winhauer T., Jaeger S., Valentin K.-U., Zetsche K.; RT "Structural similarities between psbA genes from red and brown algae."; RL Curr. Genet. 20:177-180(1991). 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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01379}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein CC {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2) CC are entirely coordinated by water. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01379}. CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. CC {ECO:0000255|HAMAP-Rule:MF_01379}. 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; X55364; CAA39049.1; -; Genomic_DNA. DR PIR; S32577; S32577. DR AlphaFoldDB; P24625; -. DR SMR; P24625; -. 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; Chlorophyll; Chloroplast; Chromophore; Electron transport; KW Herbicide resistance; Iron; Magnesium; Manganese; Membrane; Metal-binding; KW Oxidoreductase; Photosynthesis; Photosystem II; Plastid; Thylakoid; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..344 FT /note="Photosystem II protein D1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT /id="PRO_0000090424" FT PROPEP 345..360 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT /id="PRO_0000316505" FT TRANSMEM 29..46 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT TRANSMEM 118..133 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT TRANSMEM 142..156 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT TRANSMEM 197..218 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT TRANSMEM 274..288 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT REGION 264..265 FT /note="Quinone (B)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 118 FT /note="Magnesium (chlorophyll-a ChlzD1 axial ligand); via FT tele nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 170 FT /note="Ca in calcium-manganese-oxide [Ca-4Mn-5O]" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 170 FT /note="Mn 4 in calcium-manganese-oxide [Ca-4Mn-5O]" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 189 FT /note="Mn 1 in calcium-manganese-oxide [Ca-4Mn-5O]" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 198 FT /note="Magnesium (chlorophyll-a PD1 axial ligand); via tele FT nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 215 FT /note="Iron; shared with heterodimeric partner; via tele FT nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 272 FT /note="Iron; shared with heterodimeric partner; via tele FT nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 332 FT /note="Mn 1 in calcium-manganese-oxide [Ca-4Mn-5O]; via FT tele nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 333 FT /note="Mn 3 in calcium-manganese-oxide [Ca-4Mn-5O]" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 333 FT /note="Mn 4 in calcium-manganese-oxide [Ca-4Mn-5O]" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 342 FT /note="Mn 1 in calcium-manganese-oxide [Ca-4Mn-5O]" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 342 FT /note="Mn 2 in calcium-manganese-oxide [Ca-4Mn-5O]" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 344 FT /note="Ca in calcium-manganese-oxide [Ca-4Mn-5O]; via FT carboxylate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 344 FT /note="Mn 2 in calcium-manganese-oxide [Ca-4Mn-5O]; via FT carboxylate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 126 FT /note="Pheophytin D1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 215 FT /note="Quinone (B)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT SITE 161 FT /note="Tyrosine radical intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT SITE 190 FT /note="Stabilizes free radical intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT SITE 344..345 FT /note="Cleavage; by CTPA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" SQ SEQUENCE 360 AA; 39681 MW; 288EDE4685061F5F CRC64; MTATLERRES ASLWARFCTW ITMNENRLYI GWFGVVMIPT LLTATSVFII ACFAAPPVDI DGIREPVAGS LLYGNNIISG AIIPSSAAIG IHFYPIWEAA SLDEWLYNGG PYQLIVLHFL LGVCCYIGRE WEFSYRLGMR PWISVAFTAP VVAASAVFLV YPIGQGSFSD GMPLGISGTF NFMLVFQAEH NILMHPLHQL GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANNGYKFG QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLGLWPV VGIWFTSMSV STMAFNLNGF NFNQSVVDSQ GRVINTWADI LNRANLGMEV MHERNAHNFP LDLASNESLP LALVAPAING //