ID   A0A0A0PFU7_9ROSI        Unreviewed;       353 AA.
AC   A0A0A0PFU7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Photosystem II D2 protein {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004333};
DE            Short=PSII D2 protein {ECO:0000256|HAMAP-Rule:MF_01383};
DE            EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01383};
DE   AltName: Full=Photosystem Q(A) protein {ECO:0000256|HAMAP-Rule:MF_01383};
GN   Name=psbD {ECO:0000256|HAMAP-Rule:MF_01383,
GN   ECO:0000313|EMBL:AHH80571.1};
OS   Erodium gruinum.
OG   Plastid {ECO:0000313|EMBL:AHH80571.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Geraniales; Geraniaceae; Erodium.
OX   NCBI_TaxID=337380 {ECO:0000313|EMBL:AHH80571.1};
RN   [1] {ECO:0000313|EMBL:AHH80571.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Blazier J.C., Jansen R.K.;
RT   "Plastid genome evolution in Erodium.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001833, ECO:0000256|HAMAP-
CC         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:0000256|HAMAP-Rule:MF_01383}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01383}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01383}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC       are entirely coordinated by water. {ECO:0000256|HAMAP-Rule:MF_01383}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000256|ARBA:ARBA00008204, ECO:0000256|HAMAP-Rule:MF_01383,
CC       ECO:0000256|RuleBase:RU004331}.
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DR   EMBL; KF804069; AHH80571.1; -; Genomic_DNA.
DR   RefSeq; YP_009111560.1; NC_025907.1.
DR   AlphaFoldDB; A0A0A0PFU7; -.
DR   GeneID; 22548172; -.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule.
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; Photosystem II protein D1-like; 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   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   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP-
KW   Rule:MF_01383};
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP-
KW   Rule:MF_01383};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_01383};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01383};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01383};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01383};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01383}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01383};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_01383};
KW   Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW   Rule:MF_01383}; Plastid {ECO:0000313|EMBL:AHH80571.1};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01383};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01383};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01383};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01383}.
FT   TRANSMEM        28..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        267..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         118
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:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         130
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         143
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         198
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:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         215
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         215
FT                   /ligand="a plastoquinone"
FT                   /ligand_id="ChEBI:CHEBI:17757"
FT                   /ligand_label="Q(A)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         262
FT                   /ligand="a plastoquinone"
FT                   /ligand_id="ChEBI:CHEBI:17757"
FT                   /ligand_label="Q(A)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         269
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
SQ   SEQUENCE   353 AA;  39515 MW;  30CBC93752867B06 CRC64;
     MTIALGKFTK DENDLFDIMD DWLRRDRFVF VGWSGLLLFP CAYFALGGWF TGTTFVTSWY
     THGLASSYLE GCNFLTAAVS TPANSLAHSL LLLWGPEAQG DLTRWCQLGG LWTFVALHGA
     FGLIGFMLRQ FELARSVQLR PYNAIAFSGP IAVFVSVFLI YPLGQSGWFF APSFGVAAIF
     RFILFFQGFH NWTLNPFHMM GVAGVLGAAL LCAIHGATVE NTLFEDGDGA NTFRAFNPTQ
     AEETYSMVTA NRFWSQIFGV AFSNKRWLHF FMLFVPVTGL WMSALGVVGL ALNLRAYDFV
     SQEIRAAEDP EFETFYTKNI LLNEGIRAWM AAQDQPHENL IFPEEVLPRG NAL
//