ID   A0A0A0PFU7_9ROSI        Unreviewed;       353 AA.
AC   A0A0A0PFU7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   25-MAY-2022, entry version 26.
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/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: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   -!- 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:0000256|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: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   GeneID; 22548172; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
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   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   METAL           118
FT                   /note="Magnesium (chlorophyll-a ChlzD2 axial ligand); via
FT                   tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   METAL           198
FT                   /note="Magnesium (chlorophyll-a PD2 axial ligand); via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   METAL           215
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   METAL           269
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         130
FT                   /note="Pheophytin D2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         143
FT                   /note="Pheophytin D2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         215
FT                   /note="Plastoquinone Q(A)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT   BINDING         262
FT                   /note="Plastoquinone Q(A); via amide nitrogen"
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
//