ID   PSBD_ANGEV              Reviewed;         353 AA.
AC   A2T330;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
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   Angiopteris evecta (Mule's foot fern) (Polypodium evectum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Marattiidae; Marattiales; Marattiaceae; Angiopteris.
OX   NCBI_TaxID=13825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Roper J.M., Hansen S.K., Wolf P.G., Karol K.G., Mandoli D.F.,
RA   Everett K.D.E., Kuehl J., Boore J.L.;
RT   "The complete plastid genome sequence of Angiopteris evecta (G. Forst.)
RT   Hoffm. (Marattiaceae).";
RL   Am. Fern J. 97:95-106(2007).
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 + 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, 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   -!- 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   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000255|HAMAP-Rule:MF_01383}.
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DR   EMBL; DQ821119; ABG79597.1; -; Genomic_DNA.
DR   RefSeq; YP_001023698.1; NC_008829.1.
DR   AlphaFoldDB; A2T330; -.
DR   SMR; A2T330; -.
DR   GeneID; 4788187; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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; PHOTOSYSTEM II PROTEIN D1; 1.
DR   PANTHER; PTHR33149:SF12; 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; Chlorophyll; Chloroplast; Chromophore; Electron transport;
KW   Iron; Magnesium; Membrane; Metal-binding; Oxidoreductase; Phosphoprotein;
KW   Photosynthesis; Photosystem II; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P56761"
FT   CHAIN           2..353
FT                   /note="Photosystem II D2 protein"
FT                   /id="PRO_0000359621"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        125..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        153..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        279..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
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:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         130
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         143
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D2"
FT                   /evidence="ECO:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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: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"
SQ   SEQUENCE   353 AA;  39403 MW;  2736F4183089AC63 CRC64;
     MTIAIGKSSK EPKDLFDSMD DWLRRDRFVF VGWSGLLLFP CAYFALGGWF TGTTFVTSWY
     THGLASSYLE GCNFLTAAVS TPANSLAHSL LLLWGPEAQG DFTRWCQLGG LWTFVALHGS
     FGLIGFMLRQ FELARSVQLR PYNAIAFSGP ISVFVSVSLI YPLGQAGWFF APSFGVAAIF
     RFILFFQGFH NWTLNPFHMM GVAGVLGAAL LCAIHGATVE NTLFEDGDGA NTFRAFNPTQ
     SEETYSMVTA NRFWSQIFGV AFSNKRWLHF FMLFVPVTGL WMSAIGVVGL ALNLRAYDFV
     SQEIRAAEDP EFETFYTKNI LLNEGIRAWM AAQDQPHENL VFPEEVLPRG NAL
//