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PSBD_GALSU
ID   PSBD_GALSU              Reviewed;         351 AA.
AC   P28253;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 115.
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   Galdieria sulphuraria (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Galdieria.
OX   NCBI_TaxID=130081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=14-1-1 / Isolate 107.79/Goettingen;
RX   PubMed=1558950; DOI=10.1007/bf00020019;
RA   Kessler U., Maid U., Zetsche K.;
RT   "An equivalent to bacterial ompR genes is encoded on the plastid genome of
RT   red algae.";
RL   Plant Mol. Biol. 18:777-780(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=14-1-1 / Isolate 107.79/Goettingen;
RX   PubMed=1511125; DOI=10.1007/bf00040531;
RA   Maid U., Zetsche K.;
RT   "A 16 kb small single-copy region separates the plastid DNA inverted repeat
RT   of the unicellular red alga Cyanidium caldarium: physical mapping of the
RT   IR-flanking regions and nucleotide sequences of the psbD, psbC, rps16, 5S
RT   rRNA and rpl21 genes.";
RL   Plant Mol. Biol. 19:1001-1010(1992).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01383}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01383}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC       are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01383}.
CC   -!- MISCELLANEOUS: Although originally identified as Cyanidium caldarium,
CC       these sequences derive from Galdieria sulphuraria. {ECO:0000305}.
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; X62578; CAA44459.1; -; Genomic_DNA.
DR   AlphaFoldDB; P28253; -.
DR   SMR; P28253; -.
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; IEA:UniProtKB-KW.
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: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   3: Inferred from homology;
KW   Chlorophyll; Chloroplast; Chromophore; Electron transport; Iron; Magnesium;
KW   Membrane; Metal-binding; Oxidoreductase; Photosynthesis; Photosystem II;
KW   Plastid; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..351
FT                   /note="Photosystem II D2 protein"
FT                   /id="PRO_0000090504"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        123..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        151..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        277..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         116
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         128
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         141
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         196
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         213
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         213
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         260
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         267
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"
SQ   SEQUENCE   351 AA;  39346 MW;  05100785E1450601 CRC64;
     MTIAIERNIQ RGLFDLVDDW LKRDRFVFIG WSGLLLFPCS YLALGAWFTG TTFVTSWYTH
     GLASSYLEGC NFLTAAVSSP ANSMGHSLLF LWGPEAQGDF TRWCQIGGLW TFTALHGAFG
     LIGFCLRQFE IARLVGIRPY NAIAFSGPIA VFVSVFLIYP LGQASWFFAP SFGVAAIFRF
     ILFLQGFHNW TLNPFHMMGV AGILGGALLC AIHGATVENT LFEDGEAANT FRAFTPTQSE
     ETYSMVTANR FWSQIFGVAF SNKRWLHFFM LFVPVTGLWT SSIGIIGLAL NLRAYDFVSQ
     ELRAAEDPEF ETFYTKNLLL NEGIRAWMAT QDQPHENFVF PEEVLPRGNA L
 
 
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