PSBE_CHLRE
ID PSBE_CHLRE Reviewed; 82 AA.
AC P48268; B7U1I0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=137c / CC-125;
RX PubMed=7803458; DOI=10.1016/0005-2728(94)90067-1;
RA Alizadeh S., Nechustai R., Barber J., Nixon P.;
RT "Nucleotide sequence of the psbE, psbF and trnM genes from the chloroplast
RT genome of Chlamydomonas reinhardtii.";
RL Biochim. Biophys. Acta 1188:439-442(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=137c / CC-125;
RX PubMed=7700232; DOI=10.1007/bf00298966;
RA Mor T.S., Ohad I., Hirschberg J., Pakrasi H.B.;
RT "An unusual organization of the genes encoding cytochrome b559 in
RT Chlamydomonas reinhardtii: psbE and psbF genes are separately transcribed
RT from different regions of the plastid chromosome.";
RL Mol. Gen. Genet. 246:600-604(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [4]
RP PROTEIN SEQUENCE OF 2-13, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=1885590; DOI=10.1016/s0021-9258(18)55345-x;
RA de Vitry C., Diner B.A., Popo J.-L.;
RT "Photosystem II particles from Chlamydomonas reinhardtii. Purification,
RT molecular weight, small subunit composition, and protein phosphorylation.";
RL J. Biol. Chem. 266:16614-16621(1991).
RN [5]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
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, ECO:0000269|PubMed:1885590}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:1885590}; Single-
CC pass membrane protein {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; X80196; CAA56487.1; -; Genomic_DNA.
DR EMBL; X79565; CAA56102.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50127.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00941.1; -; Genomic_DNA.
DR PIR; S53882; S53882.
DR RefSeq; NP_958396.1; NC_005353.1.
DR PDB; 6KAC; EM; 2.70 A; E/e=1-82.
DR PDB; 6KAD; EM; 3.40 A; E/e=1-82.
DR PDB; 6KAF; EM; 3.73 A; E/e=1-82.
DR PDBsum; 6KAC; -.
DR PDBsum; 6KAD; -.
DR PDBsum; 6KAF; -.
DR AlphaFoldDB; P48268; -.
DR SMR; P48268; -.
DR STRING; 3055.DAA00941; -.
DR PaxDb; P48268; -.
DR PRIDE; P48268; -.
DR GeneID; 2716990; -.
DR KEGG; cre:ChreCp040; -.
DR eggNOG; ENOG502S3QA; Eukaryota.
DR HOGENOM; CLU_194095_0_0_1; -.
DR InParanoid; P48268; -.
DR OrthoDB; 1506855at2759; -.
DR BioCyc; MetaCyc:CHRECP040-MON; -.
DR Proteomes; UP000006906; Chloroplast.
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; Direct protein sequencing; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Photosynthesis; Photosystem II;
KW Plastid; Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1885590"
FT CHAIN 2..82
FT /note="Cytochrome b559 subunit alpha"
FT /id="PRO_0000200304"
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 STRAND 10..13
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 21..25
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 26..39
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:6KAC"
SQ SEQUENCE 82 AA; 9304 MW; 527E3A936C921DA9 CRC64;
MAGKPVERPF SDILTSIRYW VIHSITVPAL FIAGWLFVST GLAYDVFGTP RPNEYFTEDR
QEAPLITDRF NALEQVKKLS GN
