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 28-JUN-2023, entry version 117. 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. 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/PsbD) 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: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:0009635; P:response to herbicide; IEA:UniProtKB-KW. DR CDD; cd09289; Photosystem-II_D1; 1. DR Gene3D; 1.20.85.10; Photosystem II protein D1-like; 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; PHOTOSYSTEM II PROTEIN D1; 1. DR PANTHER; PTHR33149:SF40; PHOTOSYSTEM II PROTEIN D1; 1. DR Pfam; PF00124; Photo_RC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR SUPFAM; SSF81483; Bacterial photosystem II reaction centre, L and M subunits; 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 BINDING 118 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:0000255|HAMAP-Rule:MF_01379" FT BINDING 126 FT /ligand="pheophytin a" FT /ligand_id="ChEBI:CHEBI:136840" FT /ligand_label="D1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 170 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 189 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 198 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:0000255|HAMAP-Rule:MF_01379" FT BINDING 215 FT /ligand="a quinone" FT /ligand_id="ChEBI:CHEBI:132124" FT /ligand_label="B" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 215 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 264..265 FT /ligand="a quinone" FT /ligand_id="ChEBI:CHEBI:132124" FT /ligand_label="B" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 272 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 332 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 333 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 342 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 344 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" 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 //