ID H8ZXF6_9EUGL Unreviewed; 41 AA.
AC H8ZXF6;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Cytochrome b559 subunit beta {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
DE AltName: Full=PSII reaction center subunit VI {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
GN Name=psbF {ECO:0000256|HAMAP-Rule:MF_00643,
GN ECO:0000313|EMBL:AEQ94230.1};
OS Eutreptia viridis.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEQ94230.1}.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Eutreptiales; Eutreptia.
OX NCBI_TaxID=96908 {ECO:0000313|EMBL:AEQ94230.1};
RN [1] {ECO:0000313|EMBL:AEQ94230.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22364772; DOI=10.1016/j.protis.2012.01.002;
RA Wiegert K.E., Bennett M.S., Triemer R.E.;
RT "Evolution of the chloroplast genome in photosynthetic euglenoids: a
RT comparison of Eutreptia viridis and Euglena gracilis (Euglenophyta).";
RL Protist 163:832-843(2012).
RN [2] {ECO:0000313|EMBL:AEQ94230.1}
RP NUCLEOTIDE SEQUENCE.
RA Wiegert K.E., Bennett M.S., Triemer R.E.;
RL Submitted (MAR-2013) 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_00643, ECO:0000256|RuleBase:RU004529}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00643};
CC Note=With its partner (PsbE) binds heme. PSII binds additional
CC chlorophylls, carotenoids and specific lipids. {ECO:0000256|HAMAP-
CC Rule:MF_00643};
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_00643}.
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_00643,
CC ECO:0000256|RuleBase:RU004529}; Single-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529}.
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000256|HAMAP-
CC Rule:MF_00643, ECO:0000256|RuleBase:RU004529}.
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DR EMBL; JN643723; AEQ94230.1; -; Genomic_DNA.
DR AlphaFoldDB; H8ZXF6; -.
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 HAMAP; MF_00643; PSII_PsbF; 1.
DR InterPro; IPR006241; PSII_cyt_b559_bsu.
DR InterPro; IPR006216; PSII_cyt_b559_CS.
DR InterPro; IPR013081; PSII_cyt_b559_N.
DR NCBIfam; TIGR01333; cyt_b559_beta; 1.
DR Pfam; PF00283; Cytochrom_B559; 1.
DR PIRSF; PIRSF000037; PsbF; 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:AEQ94230.1};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_00643};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_00643};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00643};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00643};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00643};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_00643};
KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW Rule:MF_00643}; Plastid {ECO:0000313|EMBL:AEQ94230.1};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00643};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00643};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00643};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00643}.
FT TRANSMEM 16..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004529"
FT DOMAIN 5..31
FT /note="Photosystem II cytochrome b559 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00283"
FT BINDING 20
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with alpha subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00643"
SQ SEQUENCE 41 AA; 4761 MW; D22657E7ED1CD070 CRC64;
MTTNKQLTYP IFTFRWLAVH ALAIPTVFFI GSISAMQFIQ R
//
