PSBD_CHLRE
ID PSBD_CHLRE Reviewed; 352 AA.
AC P06007; B7U1K4;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Photosystem II D2 protein {ECO:0000255|HAMAP-Rule:MF_01383};
DE Short=PSII D2 protein {ECO:0000255|HAMAP-Rule:MF_01383};
DE EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01383};
DE AltName: Full=Photosystem Q(A) protein {ECO:0000255|HAMAP-Rule:MF_01383};
GN Name=psbD {ECO:0000255|HAMAP-Rule:MF_01383};
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].
RX PubMed=16453694; DOI=10.1002/j.1460-2075.1986.tb04422.x;
RA Erickson J.M., Rahire M., Malnoe P., Girard-Bascou J., Pierre Y.,
RA Bennoun P., Rochaix J.-D.;
RT "Lack of the D2 protein in a Chlamydomonas reinhardtii psbD mutant affects
RT photosystem II stability and D1 expression.";
RL EMBO J. 5:1745-1754(1986).
RN [2]
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 [3]
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).
RN [4]
RP SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
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).
CC -!- FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone
CC oxidoreductase that uses light energy to abstract electrons from H(2)O,
CC generating O(2) and a proton gradient subsequently used for ATP
CC formation. It consists of a core antenna complex that captures photons,
CC and an electron transfer chain that converts photonic excitation into a
CC charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer
CC binds P680, the primary electron donor of PSII as well as several
CC subsequent electron acceptors. D2 is needed for assembly of a stable
CC PSII complex. {ECO:0000255|HAMAP-Rule:MF_01383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2;
CC Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01383};
CC -!- COFACTOR:
CC Note=The D1/D2 heterodimer binds P680, chlorophylls that are the
CC primary electron donor of PSII, and subsequent electron acceptors. It
CC shares a non-heme iron and each subunit binds pheophytin, quinone,
CC additional chlorophylls, carotenoids and lipids. There is also a Cl(-1)
CC ion associated with D1 and D2, which is required for oxygen evolution.
CC The PSII complex binds additional chlorophylls, carotenoids and
CC specific lipids. {ECO:0000255|HAMAP-Rule:MF_01383};
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC evolving complex and a large number of cofactors. It forms dimeric
CC complexes. {ECO:0000255|HAMAP-Rule:MF_01383,
CC ECO:0000269|PubMed:1885590}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:1885590}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01383}.
CC -!- PTM: Phosphorylated in vitro (PubMed:1885590).
CC {ECO:0000269|PubMed:1885590}.
CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01383}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000255|HAMAP-Rule:MF_01383}.
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DR EMBL; X04147; CAA27766.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50151.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00964.1; -; Genomic_DNA.
DR PIR; A25466; A25466.
DR RefSeq; NP_958420.1; NC_005353.1.
DR PDB; 6KAC; EM; 2.70 A; D/d=1-352.
DR PDB; 6KAD; EM; 3.40 A; D/d=1-352.
DR PDB; 6KAF; EM; 3.73 A; D/d=1-352.
DR PDBsum; 6KAC; -.
DR PDBsum; 6KAD; -.
DR PDBsum; 6KAF; -.
DR AlphaFoldDB; P06007; -.
DR SMR; P06007; -.
DR STRING; 3055.DAA00964; -.
DR PaxDb; P06007; -.
DR PRIDE; P06007; -.
DR GeneID; 2716961; -.
DR KEGG; cre:ChreCp064; -.
DR eggNOG; ENOG502QWJF; Eukaryota.
DR HOGENOM; CLU_077965_0_0_1; -.
DR InParanoid; P06007; -.
DR OrthoDB; 801765at2759; -.
DR BioCyc; MetaCyc:CHRECP064-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:0009523; C:photosystem II; IBA:GO_Central.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR CDD; cd09288; Photosystem-II_D2; 1.
DR Gene3D; 1.20.85.10; -; 1.
DR HAMAP; MF_01383; PSII_PsbD_D2; 1.
DR InterPro; IPR036854; Photo_II_D1/D2_sf.
DR InterPro; IPR000484; Photo_RC_L/M.
DR InterPro; IPR005868; PSII_PsbD/D2.
DR PANTHER; PTHR33149; PTHR33149; 1.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; SSF81483; 1.
DR TIGRFAMs; TIGR01152; psbD; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chlorophyll; Chloroplast; Chromophore;
KW Electron transport; Iron; Magnesium; Membrane; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P56761"
FT CHAIN 2..352
FT /note="Photosystem II D2 protein"
FT /id="PRO_0000090500"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT TRANSMEM 124..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT TRANSMEM 152..165
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT TRANSMEM 278..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT BINDING 117
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="ChlzD2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT BINDING 129
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT BINDING 142
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT BINDING 197
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="PD2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT BINDING 214
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="Q(A)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT BINDING 214
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT BINDING 261
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="Q(A)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P56761"
FT MOD_RES 2
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P56761"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 37..51
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 95..99
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 109..135
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 195..220
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 264..290
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 314..333
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:6KAC"
SQ SEQUENCE 352 AA; 39447 MW; 81046BC2D36A2C61 CRC64;
MTIAIGTYQE KRTWFDDADD WLRQDRFVFV GWSGLLLFPC AYFALGGWLT GTTFVTSWYT
HGLATSYLEG CNFLTAAVST PANSMAHSLL FVWGPEAQGD FTRWCQLGGL WAFVALHGAF
GLIGFMLRQF EIARSVNLRP YNAIAFSAPI AVFVSVFLIY PLGQSGWFFA PSFGVAAIFR
FILFFQGFHN WTLNPFHMMG VAGVLGAALL CAIHGATVEN TLFEDGDGAN TFRAFNPTQA
EETYSMVTAN RFWSQIFGVA FSNKRWLHFF MLLVPVTGLW MSAIGVVGLA LNLRAYDFVS
QEIRAAEDPE FETFYTKNIL LNEGIRAWMA AQDQPHERLV FPEEVLPRGN AL
