ID Q09W58_9MARC Unreviewed; 353 AA. AC Q09W58; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 06-MAR-2013, entry version 40. DE RecName: Full=Photosystem Q(B) protein; DE EC=1.10.3.9; DE AltName: Full=32 kDa thylakoid membrane protein; DE AltName: Full=Photosystem II protein D1; GN Name=psbA; OS Lophocolea heterophylla. OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta; OC Jungermanniopsida; Jungermanniidae; Jungermanniales; Lophocoleineae; OC Lophocoleaceae; Lophocolea. OX NCBI_TaxID=3207; RN [1] RP NUCLEOTIDE SEQUENCE. RA Forrest L.L., Davis E.C., Long D.G., Crandall-Stotler B.J., Clark A., RA Hollingsworth M.L.; RT "Unraveling the evolutionary history of the Liverworts RT (Marchantiophyta): Multiple taxa, genomes and analyses."; RL Bryologist 109:303-334(2006). CC -!- FUNCTION: This is one of the two reaction center proteins of CC photosystem II (PSII) (By similarity). CC -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2 CC plastoquinol. CC -!- COFACTOR: The PsbA/B heterodimer binds P680, the primary electron CC donor of PSII. It shares a non-heme iron and each subunit binds CC additional chlorophylls and pheophytin. PsbA provides most of the CC ligands for the Mn-cluster of the oxygen-evolving complex (By CC similarity). CC -!- SUBUNIT: The PsbA/B heterodimer binds the P680 chlorophylls and CC subsequent electron acceptors. PSII consists of a core antenna CC complex that captures photons and an electron transfer chain that CC converts photonic excitation into a charge separation. PSII forms CC dimeric complexes (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; CC Multi-pass membrane protein (By similarity). CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil CC bind to Q(B) and block electron transport (By similarity). CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. 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; DQ268999; ABD85030.1; -; Genomic_DNA. DR ProteinModelPortal; Q09W58; -. DR SMR; Q09W58; 10-344. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0030076; C:light-harvesting complex; IEA:InterPro. DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW. 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:HAMAP. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. 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 Gene3D; 1.20.85.10; -; 1. DR HAMAP; MF_01379; PSII_PsbA_D1; 1; -. DR InterPro; IPR000484; Photo_RC_L/M. DR InterPro; IPR005867; PSII_D1. DR Pfam; PF00124; Photo_RC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR SUPFAM; SSF81483; Photo_RC_L/M; 1. DR TIGRFAMs; TIGR01151; psbA; 1. DR PROSITE; PS00244; REACTION_CENTER; 1. PE 3: Inferred from homology; KW Acetylation; Chloroplast; Electron transport; Herbicide resistance; KW Iron; Membrane; Metal-binding; Oxidoreductase; Phosphoprotein; KW Photosynthesis; Photosystem II; Plastid; Thylakoid; Transmembrane; KW Transmembrane helix; Transport. FT TRANSMEM 36 56 Helical; (By similarity). FT TRANSMEM 109 129 Helical; (By similarity). FT TRANSMEM 141 164 Helical; (By similarity). FT TRANSMEM 192 218 Helical; (By similarity). FT TRANSMEM 269 289 Helical; (By similarity). FT METAL 215 215 Iron; shared with heterodimeric partner FT (By similarity). FT METAL 272 272 Iron; shared with heterodimeric partner FT (By similarity). FT SITE 344 345 Cleavage; by CtpA (By similarity). FT MOD_RES 2 2 N-acetylthreonine (By similarity). FT MOD_RES 2 2 Phosphothreonine (By similarity). SQ SEQUENCE 353 AA; 38777 MW; 390E08D350D48E22 CRC64; MTATLERRES ASIWGRFCDW ITSTENRLYI GWFGVVMIPT LLTATSVFII AFIAAPPVDI DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAAAAVFLI YPIGQGSFSD GMPLGISGTF NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANAGYKFG QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAAIEAPI TNG //