ID B0Z561_OENGL Unreviewed; 83 AA.
AC B0Z561;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 80.
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:ABX10054.1};
OS Oenothera glazioviana (Large-flowered evening primrose) (Oenothera
OS erythrosepala).
OG Plastid {ECO:0000313|EMBL:ABX10054.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX NCBI_TaxID=482428 {ECO:0000313|EMBL:ABX10054.1};
RN [1] {ECO:0000313|EMBL:ABX10054.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R/r-lamarckiana Sweden {ECO:0000313|EMBL:ABX10054.1};
RX PubMed=18614526; DOI=10.1093/molbev/msn149;
RA Greiner S., Wang X., Herrmann R.G., Rauwolf U., Mayer K., Haberer G.,
RA Meurer J.;
RT "The complete nucleotide sequences of the 5 genetically distinct plastid
RT genomes of Oenothera, subsection Oenothera: II. A microevolutionary view
RT using bioinformatics and formal genetic data.";
RL Mol. Biol. Evol. 25:2019-2030(2008).
RN [2] {ECO:0000313|EMBL:ABX10054.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R/r-lamarckiana Sweden {ECO:0000313|EMBL:ABX10054.1};
RX PubMed=18299283; DOI=10.1093/nar/gkn081;
RA Greiner S., Wang X., Rauwolf U., Silber M.V., Mayer K., Meurer J.,
RA Haberer G., Herrmann R.G.;
RT "The complete nucleotide sequences of the five genetically distinct plastid
RT genomes of Oenothera, subsection Oenothera: I. sequence evaluation and
RT plastome evolution.";
RL Nucleic Acids Res. 36:2366-2378(2008).
RN [3] {ECO:0000313|EMBL:ABX10054.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Blandina de Vries {ECO:0000313|EMBL:ALR86184.1}, Deserens de
RC Vries {ECO:0000313|EMBL:ALR86268.1}, R/r-lamarckiana Sweden
RC {ECO:0000313|EMBL:ABX10054.1}, and Vet/vet-lamarckiana de Vries
RC {ECO:0000313|EMBL:ALR86436.1};
RX PubMed=27053421; DOI=10.1105/tpc.15.00879;
RA Massouh A., Schubert J., Yaneva-Roder L., Ulbricht-Jones E.S., Zupok A.,
RA Johnson M.T., Wright S.I., Pellizzer T., Sobanski J., Bock R., Greiner S.;
RT "Spontaneous Chloroplast Mutants Mostly Occur by Replication Slippage and
RT Show a Biased Pattern in the Plastome of Oenothera.";
RL Plant Cell 28:911-929(2016).
RN [4] {ECO:0000313|EMBL:QBE85689.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Decipiens de Vries {ECO:0000313|EMBL:QBE85689.1};
RA Garbsch F., Greiner S.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ABX10054.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R/r-lamarckiana Sweden {ECO:0000313|EMBL:ABX10054.1};
RX PubMed=30833407; DOI=.1073/pnas.1811661116;
RA Sobanski J., Giavalisco P., Fischer A., Kreiner J.M., Walther D.,
RA Schottler M.A., Pellizzer T., Golczyk H., Obata T., Bock R., Sears B.B.,
RA Greiner S.;
RT "Chloroplast competition is controlled by lipid biosynthesis in evening
RT primroses.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:5665-5674(2019).
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 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: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_00642}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00642}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid, chloroplast
CC thylakoid membrane {ECO:0000256|RuleBase:RU004529}; Single-pass
CC membrane protein {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; EU262890; ABX10054.1; -; Genomic_DNA.
DR EMBL; KT881171; ALR86184.1; -; Genomic_DNA.
DR EMBL; KT881172; ALR86268.1; -; Genomic_DNA.
DR EMBL; KT881174; ALR86436.1; -; Genomic_DNA.
DR EMBL; MH168559; QBE85689.1; -; Genomic_DNA.
DR RefSeq; YP_001687300.1; NC_010360.2.
DR AlphaFoldDB; B0Z561; -.
DR SMR; B0Z561; -.
DR GeneID; 5955337; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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; 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; IPR006216; PSII_cyt_b559_CS.
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.
DR PROSITE; PS00537; CYTOCHROME_B559; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|RuleBase:RU004529, ECO:0000313|EMBL:ABX10054.1};
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:ABX10054.1};
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 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004529"
FT DOMAIN 6..34
FT /note="Photosystem II cytochrome b559 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00283"
FT DOMAIN 42..79
FT /note="Photosystem II cytochrome b559 alpha subunit lumenal
FT region"
FT /evidence="ECO:0000259|Pfam:PF00284"
FT BINDING 23
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; 9387 MW; F1E3918BCABACDDE CRC64;
MSGSTGERSF ADIITSIRYW VIHSITIPSL FIAGWLFVST GLAYDVFGSP RPNEYFTESR
QGIPLITGRF DSLEQLDEFS RSF
//
