ID A0A0S2GKS4_9APIA Unreviewed; 83 AA. AC A0A0S2GKS4; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 12-AUG-2020, entry version 21. 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:ALN96839.1}; OS Angelica decursiva. OG Plastid; Chloroplast {ECO:0000313|EMBL:ALN96839.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade; OC Selineae; Angelica. OX NCBI_TaxID=52491 {ECO:0000313|EMBL:ALN96839.1}; RN [1] {ECO:0000313|EMBL:ALN96839.1} RP NUCLEOTIDE SEQUENCE. RA Choi S.A., Kim Y., Lee W.K., Kim K.Y., Kim J.H., Seong R.S.; RT "The complete chloroplast genome of the medical plant Angelica decursiva RT (Umbelliferae) in Peucedani Radix."; RL Submitted (SEP-2015) 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 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. CC {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|HAMAP-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 is CC composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, CC PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, CC Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex CC and a large number of cofactors. It forms dimeric complexes. CC {ECO:0000256|HAMAP-Rule:MF_00642}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00642, CC ECO:0000256|RuleBase:RU004529}; Single-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_00642, 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; KT781591; ALN96839.1; -; Genomic_DNA. DR SMR; A0A0S2GKS4; -. 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:0009539; C:photosystem II reaction center; IEA:InterPro. DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009767; P:photosynthetic electron transport chain; IEA:InterPro. 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, ECO:0000313|EMBL:ALN96839.1}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP- KW Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP- KW Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; KW Plastid {ECO:0000313|EMBL:ALN96839.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00642}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00642, ECO:0000256|RuleBase:RU004529}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00642, KW ECO:0000256|RuleBase:RU004529}. FT TRANSMEM 20..44 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004529" FT DOMAIN 6..34 FT /note="Cytochrom_B559" FT /evidence="ECO:0000259|Pfam:PF00283" FT DOMAIN 42..79 FT /note="Cytochrom_B559a" FT /evidence="ECO:0000259|Pfam:PF00284" FT METAL 23 FT /note="Iron (heme axial ligand); shared with beta subunit" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00642" SQ SEQUENCE 83 AA; 9424 MW; ED325C8805BACDDE CRC64; MSGSTGERSF ADIITSIRYW VIHSITIPSL FIAGWLFVST GLAYDVFGSP RPNEYFTENR QGIPLITGRF DPLEQLDEFS RSF //