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 04-NOV-2026, entry version 171. 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/PsbD) 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 + 4 hnu + 2 H2O = 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, Psb30/Ycf12, at least 3 peripheral proteins of the CC oxygen-evolving complex and a large number of cofactors. It forms CC dimeric 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}. 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; 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 PDB; 8KDE; EM; 2.60 A; D=1-352. DR PDB; 8R2I; EM; 2.90 A; D=3-352. DR PDB; 8ZEE; EM; 2.90 A; D=1-352. DR PDB; 9HEI; EM; 2.92 A; D=5-352. DR PDB; 9IIU; EM; 2.98 A; D=4-352. DR PDB; 9IMN; EM; 2.97 A; D/d=2-352. DR PDB; 9IOX; EM; 3.30 A; D/d=2-352. DR PDB; 9IS4; EM; 2.90 A; D/d=2-352. DR AlphaFoldDB; P06007; -. DR EMDB; EMD-18848; -. DR EMDB; EMD-37133; -. DR EMDB; EMD-52077; -. DR EMDB; EMD-60026; -. DR EMDB; EMD-60605; -. DR EMDB; EMD-60694; -. DR EMDB; EMD-60748; -. DR EMDB; EMD-60830; -. DR EMDB; EMD-9955; -. DR EMDB; EMD-9956; -. DR EMDB; EMD-9957; -. DR SMR; P06007; -. DR FunCoup; P06007; 230. DR STRING; 3055.P06007; -. DR PaxDb; 3055-P06007; -. DR GeneID; 2716961; -. DR KEGG; cre:ChreCp064; -. DR eggNOG; ENOG502QWJF; Eukaryota. DR HOGENOM; CLU_077965_0_0_1; -. DR InParanoid; P06007; -. DR BioCyc; CHLAMY:CHRECP064-MONOMER; -. DR BioCyc; MetaCyc:CHRECP064-MONOMER; -. DR BRENDA; 1.10.3.9; 1318. DR Proteomes; UP000006906; Chloroplast. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009523; C:photosystem II; IBA:GO_Central. DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule. DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule. 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 FunFam; 1.20.85.10:FF:000001; photosystem II D2 protein-like; 1. DR Gene3D; 1.20.85.10; Photosystem II protein D1-like; 1. DR HAMAP; MF_01383; PSII_PsbD_D2; 1. DR InterPro; IPR055266; D1/D2. DR InterPro; IPR036854; Photo_II_D1/D2_sf. DR InterPro; IPR000484; Photo_RC_L/M. DR InterPro; IPR055265; Photo_RC_L/M_CS. DR InterPro; IPR005868; PSII_PsbD/D2. DR NCBIfam; TIGR01152; psbD; 1. DR PANTHER; PTHR33149:SF12; PHOTOSYSTEM II D2 PROTEIN; 1. DR PANTHER; PTHR33149; PHOTOSYSTEM II PROTEIN D1; 1. DR Pfam; PF00124; Photo_RC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR SUPFAM; SSF81483; Bacterial photosystem II reaction centre, L and M subunits; 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 10..13 FT /evidence="ECO:0007829|PDB:6KAD" FT HELIX 14..22 FT /evidence="ECO:0007829|PDB:8KDE" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 31..53 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:8KDE" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:6KAC" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:6KAD" FT TURN 95..99 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 101..107 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 109..135 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 141..154 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 155..159 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 160..163 FT /evidence="ECO:0007829|PDB:8KDE" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 175..189 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 195..219 FT /evidence="ECO:0007829|PDB:8KDE" FT STRAND 221..223 FT /evidence="ECO:0007829|PDB:8KDE" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:8KDE" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 246..256 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 264..290 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 299..307 FT /evidence="ECO:0007829|PDB:8KDE" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:9HEI" FT HELIX 314..333 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:8KDE" FT TURN 343..345 FT /evidence="ECO:0007829|PDB:8KDE" FT HELIX 349..351 FT /evidence="ECO:0007829|PDB:8KDE" 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 //