ID E9KJA8_9ORYZ Unreviewed; 104 AA.
AC E9KJA8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:ADD63051.1};
OS Potamophila parviflora.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ADD63051.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Zizaniinae; Potamophila.
OX NCBI_TaxID=66034 {ECO:0000313|EMBL:ADD63051.1};
RN [1] {ECO:0000313|EMBL:ADD63051.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20796245; DOI=10.1111/j.1467-7652.2010.00558.x;
RA Nock C.J., Waters D.L., Edwards M.A., Bowen S.G., Rice N., Cordeiro G.M.,
RA Henry R.J.;
RT "Chloroplast genome sequences from total DNA for plant identification.";
RL Plant Biotechnol. J. 9:328-333(2011).
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: 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}.
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DR EMBL; GU592210; ADD63051.1; -; Genomic_DNA.
DR AlphaFoldDB; E9KJA8; -.
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:SF13; CYTOCHROME B559 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR33391; CYTOCHROME B559 SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00283; Cytochrom_B559; 1.
DR Pfam; PF00284; Cytochrom_B559a; 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:ADD63051.1};
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:ADD63051.1};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, 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 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004529"
FT DOMAIN 27..55
FT /note="Photosystem II cytochrome b559 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00283"
FT DOMAIN 63..100
FT /note="Photosystem II cytochrome b559 alpha subunit lumenal
FT region"
FT /evidence="ECO:0000259|Pfam:PF00284"
FT BINDING 44
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 104 AA; 11811 MW; 1DB5D8EE4D59DF5D CRC64;
MIPSFTESIP FLNVQKFGEL SMSGSTGERS FADIITSIRY WVIHSITIPS LFIAGWLFVS
TGLAYDVFGS PRPNEYFTES RQGIPLITDR FDSLEQLDEF SRSF
//
