ID K9ZDS6_ANACC Unreviewed; 360 AA. AC K9ZDS6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 29-MAY-2024, entry version 63. DE RecName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379}; 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 OrderedLocusNames=Anacy_0955 {ECO:0000313|EMBL:AFZ56530.1}, Anacy_5146 GN {ECO:0000313|EMBL:AFZ60480.1}; OS Anabaena cylindrica (strain ATCC 27899 / PCC 7122). OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ56530.1, ECO:0000313|Proteomes:UP000010474}; RN [1] {ECO:0000313|EMBL:AFZ56530.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7122 {ECO:0000313|EMBL:AFZ56530.1}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N., RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A., RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.; RT "Finished chromosome of genome of Anabaena cylindrica PCC 7122."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000010474} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A., RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K., RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S., RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity-driven RT genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). 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:0000256|ARBA:ARBA00037683, CC 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 -!- 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, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), CC PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. CC {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {ECO:0000256|ARBA:ARBA00004636, ECO:0000256|HAMAP-Rule:MF_01379}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004636, CC ECO:0000256|HAMAP-Rule:MF_01379}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. 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: Cyanobacteriota usually contain more than 2 copies of CC the psbA gene. {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; CP003659; AFZ56530.1; -; Genomic_DNA. DR EMBL; CP003659; AFZ60480.1; -; Genomic_DNA. DR RefSeq; WP_015213182.1; NC_019771.1. DR AlphaFoldDB; K9ZDS6; -. DR SMR; K9ZDS6; -. DR STRING; 272123.Anacy_0955; -. DR KEGG; acy:Anacy_0955; -. DR KEGG; acy:Anacy_5146; -. DR PATRIC; fig|272123.3.peg.1044; -. DR eggNOG; ENOG502Z87P; Bacteria. DR HOGENOM; CLU_054206_1_0_3; -. DR OrthoDB; 505356at2; -. DR Proteomes; UP000010474; Chromosome. DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW. DR GO; GO:0031676; C:plasma membrane-derived 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:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC. 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; 2. 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 NCBIfam; TIGR01151; psbA; 1. DR PANTHER; PTHR33149; PHOTOSYSTEM II PROTEIN D1; 1. DR PANTHER; PTHR33149:SF12; 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 PROSITE; PS00244; REACTION_CENTER; 1. PE 3: Inferred from homology; 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}; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP- KW Rule:MF_01379}; Electron transport {ECO:0000256|HAMAP-Rule:MF_01379}; KW Herbicide resistance {ECO:0000256|ARBA:ARBA00022646, ECO:0000256|HAMAP- KW Rule:MF_01379}; Iron {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 Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_01379}; Photosystem II {ECO:0000256|HAMAP-Rule:MF_01379}; KW Reference proteome {ECO:0000313|Proteomes:UP000010474}; 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}; Transport {ECO:0000256|HAMAP-Rule:MF_01379}. FT CHAIN 1..344 FT /note="Photosystem II protein D1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT /id="PRO_5039765231" FT PROPEP 345..360 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT /id="PRO_5039765232" FT TRANSMEM 29..55 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 111..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 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 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:0000256|HAMAP-Rule:MF_01379" FT BINDING 126 FT /ligand="pheophytin a" FT /ligand_id="ChEBI:CHEBI:136840" FT /ligand_label="D1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 170 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 189 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01379" FT BINDING 215 FT /ligand="a quinone" FT /ligand_id="ChEBI:CHEBI:132124" FT /ligand_label="B" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01379" FT BINDING 332 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 333 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 342 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT BINDING 344 FT /ligand="[CaMn4O5] cluster" FT /ligand_id="ChEBI:CHEBI:189552" 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" SQ SEQUENCE 360 AA; 39593 MW; B12899D31245F23C CRC64; MTTTIQQRST ANVWDRFCEW ITSTENRIYI GWFGVLMIPT LLAATTCFII AFIAAPPVDI DGIREPVAGS LIYGNNIISG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLVIFHFL IGCACYLGRQ WELSYRLGMR PWICVAYSAP LASATAVFLI YPIGQGSFSD GMPLGISGTF NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLVRETTET ESQNYGYKFG QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV IGIWFTALGV STMAFNLNGF NFNQSIIDSQ GRVIGTWADV INRANLGMEV MHERNAHNFP LDLAAGDVAP VALTAPAING //