ID U3R5X9_IPOPE Unreviewed; 353 AA. AC U3R5X9; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 26-NOV-2014, entry version 7. DE RecName: Full=Photosystem Q(B) protein {ECO:0000256|HAMAP-Rule:MF_01379}; DE EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01379}; DE AltName: Full=32 kDa thylakoid membrane protein {ECO:0000256|HAMAP-Rule:MF_01379}; DE AltName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379}; GN Name=psbA {ECO:0000256|HAMAP-Rule:MF_01379, GN ECO:0000313|EMBL:AGW98610.1}; OS Ipomoea pes-tigridis (Morning glory) (Convolvulus pes-tigridis). OG Plastid; Chloroplast {ECO:0000313|EMBL:AGW98610.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; OC Ipomoea. OX NCBI_TaxID=89657 {ECO:0000313|EMBL:AGW98610.1}; RN [1] {ECO:0000313|EMBL:AGW98610.1} RP NUCLEOTIDE SEQUENCE. RA Eserman L.A., Tiley G.P., Jarret R.L., Leebens-Mack J.H., Miller R.E.; RT "Phylogenetics and diversification of morning glories based on whole RT plastome sequences."; RL Am. J. Bot. 0:0-0(2013). CC -!- FUNCTION: This is one of the two reaction center proteins of CC photosystem II (PSII). {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2 CC plastoquinol. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- COFACTOR: CC Note=The PsbA/B heterodimer binds P680, the primary electron donor CC 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. CC {ECO:0000256|HAMAP-Rule:MF_01379}; 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. {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01379}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil CC bind to Q(B) and block electron transport. {ECO:0000256|HAMAP- CC 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; KF242500; AGW98610.1; -; Genomic_DNA. DR ProteinModelPortal; U3R5X9; -. DR SMR; U3R5X9; 10-344. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. 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: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-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; SSF81483; 1. DR TIGRFAMs; TIGR01151; psbA; 1. DR PROSITE; PS00244; REACTION_CENTER; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|HAMAP-Rule:MF_01379}; KW Calcium {ECO:0000256|HAMAP-Rule:MF_01379}; KW Chloroplast {ECO:0000313|EMBL:AGW98610.1}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Herbicide resistance {ECO:0000256|HAMAP-Rule:MF_01379}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004332}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01379}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01379}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Photosystem II {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Plastid {ECO:0000313|EMBL:AGW98610.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01379}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01379}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01379, KW ECO:0000256|RuleBase:RU004332}. FT TRANSMEM 36 56 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT TRANSMEM 109 129 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT TRANSMEM 141 164 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT TRANSMEM 192 218 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT TRANSMEM 269 289 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 170 170 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; calcium. {ECO:0000256|HAMAP-Rule: FT MF_01379}. FT METAL 170 170 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 1. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 189 189 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 2. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 215 215 Iron; shared with heterodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 272 272 Iron; shared with heterodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 332 332 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 2; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 333 333 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 1. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 333 333 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 3. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 342 342 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 2. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 342 342 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 4. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT METAL 344 344 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; calcium; via carboxylate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT METAL 344 344 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 4; via carboxylate. FT {ECO:0000256|HAMAP-Rule:MF_01379}. FT SITE 344 345 Cleavage; by CtpA. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT MOD_RES 2 2 N-acetylthreonine. {ECO:0000256|HAMAP- FT Rule:MF_01379}. FT MOD_RES 2 2 Phosphothreonine. {ECO:0000256|HAMAP- FT Rule:MF_01379}. SQ SEQUENCE 353 AA; 38950 MW; 7B07EBD006EC450A CRC64; MTAILERRES QSLWGRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYRFG QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAAIEAPS TNG //