ID K9ZDS6_ANACC Unreviewed; 360 AA. AC K9ZDS6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 19-JAN-2022, entry version 53. 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}; DE Flags: Precursor; 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; Cyanobacteria; 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/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: Cyanobacterial PSII is composed of 1 copy each of membrane CC proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, CC PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral CC proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms CC dimeric complexes. {ECO:0000256|ARBA:ARBA00011417, ECO:0000256|HAMAP- CC 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: Cyanobacteria usually contain more than 2 copies of the CC 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; NZ_AP018166.1. DR SMR; K9ZDS6; -. DR STRING; 272123.Anacy_0955; -. DR EnsemblBacteria; AFZ56530; AFZ56530; Anacy_0955. DR EnsemblBacteria; AFZ60480; AFZ60480; Anacy_5146. 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 OMA; CQWVTDT; -. DR OrthoDB; 382342at2; -. DR Proteomes; UP000010474; Chromosome. 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: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: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; -; 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 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|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 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_5025084060" FT PROPEP 345..360 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379" FT /id="PRO_5025084061" 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 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" 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 //