PSBE_ARATH
ID PSBE_ARATH Reviewed; 83 AA.
AC P56779; Q8HS06;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 132.
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}; OrderedLocusNames=AtCg00580;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10907847; DOI=10.1093/dnares/7.3.175;
RA Asamizu E., Nakamura Y., Sato S., Tabata S.;
RT "A large scale analysis of cDNA in Arabidopsis thaliana: generation of
RT 12,028 non-redundant expressed sequence tags from normalized and size-
RT selected cDNA libraries.";
RL DNA Res. 7:175-180(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-79.
RX PubMed=11115876; DOI=10.1104/pp.124.4.1582;
RA White J.A., Todd J., Newman T., Focks N., Girke T., de Ilarduya O.M.,
RA Jaworski J.G., Ohlrogge J.B., Benning C.;
RT "A new set of Arabidopsis expressed sequence tags from developing seeds.
RT The metabolic pathway from carbohydrates to seed oil.";
RL Plant Physiol. 124:1582-1594(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-83.
RA Graham S.W., Reeves P.A., Burns A., Olmstead R.G.;
RT "Long branches in the seed plants and the root of the angiosperms.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND RNA EDITING.
RA Battchikova N.;
RL Unpublished observations (AUG-2006).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 -!- RNA EDITING: Modified_positions=72 {ECO:0000269|Ref.5};
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|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; AP000423; BAA84402.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AV525419; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AV527712; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BE525291; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY007473; AAG26974.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_051076.1; NC_000932.1.
DR PDB; 5MDX; EM; 5.30 A; E/e=1-83.
DR PDB; 7OUI; EM; 2.79 A; E/e=1-83.
DR PDBsum; 5MDX; -.
DR PDBsum; 7OUI; -.
DR AlphaFoldDB; P56779; -.
DR SMR; P56779; -.
DR BioGRID; 29949; 23.
DR IntAct; P56779; 1.
DR STRING; 3702.ATCG00580.1; -.
DR PaxDb; P56779; -.
DR PeptideAtlas; P56779; -.
DR PRIDE; P56779; -.
DR ProteomicsDB; 226168; -.
DR GeneID; 844745; -.
DR KEGG; ath:ArthCp039; -.
DR Araport; ATCG00580; -.
DR eggNOG; ENOG502S3QA; Eukaryota.
DR HOGENOM; CLU_194095_0_0_1; -.
DR InParanoid; P56779; -.
DR OrthoDB; 1506855at2759; -.
DR BioCyc; MetaCyc:ATCG00580-MON; -.
DR PRO; PR:P56779; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P56779; baseline and differential.
DR Genevisible; P56779; AT.
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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Photosynthesis; Photosystem II; Plastid; Reference proteome;
KW RNA editing; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..83
FT /note="Cytochrome b559 subunit alpha"
FT /id="PRO_0000200298"
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"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 22..39
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:7OUI"
SQ SEQUENCE 83 AA; 9387 MW; F1E3918BCABACDDE CRC64;
MSGSTGERSF ADIITSIRYW VIHSITIPSL FIAGWLFVST GLAYDVFGSP RPNEYFTESR
QGIPLITGRF DSLEQLDEFS RSF
