ID A0A4Y5X0C8_9ROSI Unreviewed; 83 AA. AC A0A4Y5X0C8; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 13-NOV-2019, entry version 3. DE RecName: Full=Cytochrome b559 subunit alpha {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU000619}; DE AltName: Full=PSII reaction center subunit V {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; GN Name=psbE {ECO:0000256|HAMAP-Rule:MF_00642, GN ECO:0000313|EMBL:QDE13720.1}; OS Heritiera elata. OG Plastid; Chloroplast {ECO:0000313|EMBL:QDE13720.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Sterculioideae; OC Heritiera. OX NCBI_TaxID=300536 {ECO:0000313|EMBL:QDE13720.1}; RN [1] {ECO:0000313|EMBL:QDE13720.1} RP NUCLEOTIDE SEQUENCE. RA Zhou Y., Lee W., Huang Y.; RT "The complete chloroplast genome for Heritiera elata."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This b-type cytochrome is tightly associated with the CC reaction center of photosystem II (PSII). PSII is a light-driven CC water:plastoquinone oxidoreductase that uses light energy to CC abstract electrons from H(2)O, generating O(2) and a proton CC gradient subsequently used for ATP formation. It consists of a CC core antenna complex that captures photons, and an electron CC transfer chain that converts photonic excitation into a charge CC separation. {ECO:0000256|HAMAP-Rule:MF_00642, CC ECO:0000256|RuleBase:RU004529}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00642}; CC Note=With its partner (PsbF) binds heme. PSII binds additional CC chlorophylls, carotenoids and specific lipids. {ECO:0000256|HAMAP- CC Rule:MF_00642}; CC -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit. PSII CC is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, CC PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, CC PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen- CC evolving complex and a large number of cofactors. It forms dimeric CC complexes. {ECO:0000256|HAMAP-Rule:MF_00642}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00642, CC ECO:0000256|RuleBase:RU004529}. CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000256|HAMAP- CC Rule:MF_00642, ECO:0000256|RuleBase:RU004529}. 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; MK033520; QDE13720.1; -; Genomic_DNA. DR SMR; A0A4Y5X0C8; -. 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:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.5.860; -; 1. DR HAMAP; MF_00642; PSII_PsbE; 1. DR InterPro; IPR006217; PSII_cyt_b559_asu. DR InterPro; IPR037025; PSII_cyt_b559_asu_sf. DR InterPro; IPR006216; PSII_cyt_b559_CS. DR InterPro; IPR013081; PSII_cyt_b559_N. DR InterPro; IPR013082; PSII_cytb559_asu_lum. DR Pfam; PF00283; Cytochrom_B559; 1. DR Pfam; PF00284; Cytochrom_B559a; 1. DR PIRSF; PIRSF000036; PsbE; 1. DR TIGRFAMs; TIGR01332; cyt_b559_alpha; 1. DR PROSITE; PS00537; CYTOCHROME_B559; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|RuleBase:RU004529, KW ECO:0000313|EMBL:QDE13720.1}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Heme {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Photosystem II {ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Plastid {ECO:0000313|EMBL:QDE13720.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00642}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}. FT TRANSMEM 20 44 Helical. {ECO:0000256|RuleBase:RU004529}. FT DOMAIN 6 34 Cytochrom_B559. {ECO:0000259|Pfam: FT PF00283}. FT DOMAIN 42 79 Cytochrom_B559a. {ECO:0000259|Pfam: FT PF00284}. FT METAL 23 23 Iron (heme axial ligand); shared with FT beta subunit. {ECO:0000256|HAMAP-Rule: FT MF_00642}. SQ SEQUENCE 83 AA; 9397 MW; F1E3918805BACDDE CRC64; MSGSTGERSF ADIITSIRYW VIHSITIPSL FIAGWLFVST GLAYDVFGSP RPNEYFTESR QGIPLITGRF DPLEQLDEFS RSF //