ID J3JR72_9EUGL Unreviewed; 83 AA.
AC J3JR72;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Cytochrome b559 subunit alpha {ECO:0000256|HAMAP-Rule:MF_00642};
DE AltName: Full=PSII reaction center subunit V {ECO:0000256|HAMAP-Rule:MF_00642};
GN Name=psbE {ECO:0000256|HAMAP-Rule:MF_00642,
GN ECO:0000313|EMBL:AEW13034.1};
OS Strombomonas acuminata.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEW13034.1}.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Strombomonas.
OX NCBI_TaxID=201859 {ECO:0000313|EMBL:AEW13034.1};
RN [1] {ECO:0000313|EMBL:AEW13034.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23351081; DOI=10.1111/jeu.12025;
RA Wiegert K.E., Bennett M.S., Triemer R.E.;
RT "Tracing patterns of chloroplast evolution in euglenoids: contributions
RT from Colacium vesiculosum and Strombomonas acuminata (Euglenophyta).";
RL J. Eukaryot. Microbiol. 60:214-221(2013).
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}.
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 Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving
CC complex and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000256|HAMAP-Rule:MF_00642}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000256|HAMAP-Rule:MF_00642}; Single-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_00642}.
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000256|HAMAP-
CC Rule:MF_00642}.
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; JN674637; AEW13034.1; -; Genomic_DNA.
DR AlphaFoldDB; J3JR72; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
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; Photosystem II cytochrome b559, alpha subunit; 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; IPR013081; PSII_cyt_b559_N.
DR InterPro; IPR013082; PSII_cytb559_asu_lum.
DR NCBIfam; TIGR01332; cyt_b559_alpha; 1.
DR PANTHER; PTHR33391; CYTOCHROME B559 SUBUNIT BETA-RELATED; 1.
DR PANTHER; PTHR33391:SF9; CYTOCHROME B559 SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00283; Cytochrom_B559; 1.
DR Pfam; PF00284; Cytochrom_B559a; 1.
DR PIRSF; PIRSF000036; PsbE; 1.
DR SUPFAM; SSF161045; Cytochrome b559 subunits; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:AEW13034.1};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_00642};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_00642};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00642};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00642};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00642};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_00642};
KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW Rule:MF_00642}; Plastid {ECO:0000313|EMBL:AEW13034.1};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00642};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00642};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00642};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00642}.
FT TRANSMEM 19..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..36
FT /note="Photosystem II cytochrome b559 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00283"
FT DOMAIN 44..82
FT /note="Photosystem II cytochrome b559 alpha subunit lumenal
FT region"
FT /evidence="ECO:0000259|Pfam:PF00284"
FT BINDING 25
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with beta subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00642"
SQ SEQUENCE 83 AA; 9526 MW; E0EBEBC24C2B29A2 CRC64;
MAGSTGERPF SDIVVYSSIR YWVIHSVTIP SLFVAGWIFV STGLAYDIFG TPRPNEYFNE
TRQEIPLISD RFNALEQMDQ FTK
//
