ID K9ZDS6_ANACC Unreviewed; 360 AA. AC K9ZDS6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 13-FEB-2019, entry version 39. 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; 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., RA Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., RA Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., RA 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., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: Photosystem II (PSII) is a light-driven water: CC plastoquinone oxidoreductase that uses light energy to abstract CC electrons from H(2)O, generating O(2) and a proton gradient CC subsequently used for ATP formation. It consists of a core antenna CC complex that captures photons, and an electron transfer chain that CC converts photonic excitation into a charge separation. The D1/D2 CC (PsbA/PsbA) reaction center heterodimer binds P680, the primary CC electron donor of PSII as well as several subsequent electron CC acceptors. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + CC O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA- CC COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; CC EC=1.10.3.9; 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. CC It shares a non-heme iron and each subunit binds pheophytin, CC quinone, additional chlorophylls, carotenoids and lipids. D1 CC provides most of the ligands for the Mn4-Ca-O5 cluster of the CC oxygen-evolving complex (OEC). There is also a Cl(-1) ion CC associated with D1 and D2, which is required for oxygen evolution. CC The PSII complex binds additional chlorophylls, carotenoids and CC specific lipids. {ECO:0000256|HAMAP-Rule:MF_01379}; CC -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of CC membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, CC PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 CC peripheral proteins PsbO, PsbU, PsbV and a large number of CC cofactors. It forms dimeric complexes. {ECO:0000256|HAMAP- CC Rule:MF_01379}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {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 CC allow assembly of the oxygen-evolving complex and thus CC photosynthetic growth. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- PTM: Tyr-161 forms a radical intermediate that is referred to as CC redox-active TyrZ, YZ or Y-Z. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and CC ChlD2) are entirely coordinated by water. {ECO:0000256|HAMAP- CC Rule:MF_01379}. CC -!- MISCELLANEOUS: Cyanobacteria 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 CC bind in the Q(B) binding site and block subsequent electron CC transfer. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. CC {ECO:0000256|HAMAP-Rule:MF_01379, 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 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 KO; K02703; -. DR OMA; GIWFTSM; -. DR OrthoDB; 382342at2; -. DR BioCyc; ACYL272123:G1HCX-5180-MONOMER; -. DR BioCyc; ACYL272123:G1HCX-965-MONOMER; -. 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:0042651; C: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: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 {ECO:0000256|HAMAP-Rule:MF_01379}; KW Chlorophyll {ECO:0000256|HAMAP-Rule:MF_01379}; KW Chromophore {ECO:0000256|HAMAP-Rule:MF_01379}; KW Complete proteome {ECO:0000313|Proteomes:UP000010474}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_01379}; KW Herbicide resistance {ECO:0000256|HAMAP-Rule:MF_01379}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01379}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01379}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01379}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01379}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01379}; KW 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|HAMAP-Rule:MF_01379, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01379}. FT PROPEP 345 360 {ECO:0000256|HAMAP-Rule:MF_01379}. FT /FTId=PRO_5017838504. FT TRANSMEM 29 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 198 218 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 273 295 Helical. {ECO:0000256|SAM:Phobius}. FT REGION 264 265 Quinone (B). {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 118 118 Magnesium (chlorophyll-a ChlzD1 axial FT ligand); via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O]; FT calcium. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 4. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 189 189 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 198 198 Magnesium (chlorophyll-a PD1 axial FT ligand); via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 215 215 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 272 272 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 332 332 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 3. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 4. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O]; FT calcium; via carboxylate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2; via carboxylate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT BINDING 126 126 Pheophytin D1. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT BINDING 215 215 Quinone (B). {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT SITE 161 161 Tyrosine radical intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT SITE 190 190 Stabilizes free radical intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT SITE 344 345 Cleavage; by CtpA. {ECO:0000256|HAMAP- FT 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 //