PSBE_PHAAO
ID PSBE_PHAAO Reviewed; 83 AA.
AC Q3BAM3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Cytochrome b559 subunit alpha {ECO:0000255|HAMAP-Rule:MF_00642};
DE AltName: Full=PSII reaction center subunit V {ECO:0000255|HAMAP-Rule:MF_00642};
GN Name=psbE {ECO:0000255|HAMAP-Rule:MF_00642};
OS Phalaenopsis aphrodite subsp. formosana (Moth orchid).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Vandeae; Aeridinae; Phalaenopsis.
OX NCBI_TaxID=308872;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Taisugar TS-97;
RX PubMed=16207935; DOI=10.1093/molbev/msj029;
RA Chang C.-C., Lin H.-C., Lin I.-P., Chow T.-Y., Chen H.-H., Chen W.-H.,
RA Cheng C.-H., Lin C.-Y., Liu S.-M., Chang C.-C., Chaw S.-M.;
RT "The chloroplast genome of Phalaenopsis aphrodite (Orchidaceae):
RT comparative analysis of evolutionary rate with that of grasses and its
RT phylogenetic implications.";
RL Mol. Biol. Evol. 23:279-291(2006).
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:0000255|HAMAP-Rule:MF_00642}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00642};
CC Note=With its partner (PsbF) binds heme. PSII binds additional
CC chlorophylls, carotenoids and specific lipids. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00642}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00642}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00642}.
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC Rule:MF_00642}.
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DR EMBL; AY916449; AAW82517.1; -; Genomic_DNA.
DR RefSeq; YP_358595.1; NC_007499.1.
DR AlphaFoldDB; Q3BAM3; -.
DR SMR; Q3BAM3; -.
DR GeneID; 3741696; -.
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; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Photosynthesis; Photosystem II; Plastid; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..83
FT /note="Cytochrome b559 subunit alpha"
FT /id="PRO_0000233207"
FT TRANSMEM 21..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00642"
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:0000255|HAMAP-Rule:MF_00642"
SQ SEQUENCE 83 AA; 9354 MW; F1E151CBCAB2EDDE CRC64;
MSGSTGERSF ADIITSIRYW VIHSITIPSL FIAGWLFVST GLAYDVFGSP RPNEYFTESR
QGIPLITGRF DSLEQLDKFS NPF
