ID   PSBA_THAPS              Reviewed;         360 AA.
AC   A0T0W2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Photosystem II protein D1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE            Short=PSII D1 protein {ECO:0000255|HAMAP-Rule:MF_01379};
DE            EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379};
DE   AltName: Full=Photosystem II Q(B) protein {ECO:0000255|HAMAP-Rule:MF_01379};
DE   Flags: Precursor;
GN   Name=psbA {ECO:0000255|HAMAP-Rule:MF_01379};
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RX   PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA   Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA   Green B.R.;
RT   "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT   Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT   lineage.";
RL   Mol. Genet. Genomics 277:427-439(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. {ECO:0000255|HAMAP-Rule:MF_01379}.
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_01379};
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. D1 provides most of
CC       the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex
CC       (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is
CC       required for oxygen evolution. The PSII complex binds additional
CC       chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
CC       Rule:MF_01379};
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_01379}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- PTM: Tyr-161 forms a radical intermediate that is referred to as redox-
CC       active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- PTM: C-terminally processed by CTPA; processing is essential to allow
CC       assembly of the oxygen-evolving complex and thus photosynthetic growth.
CC       {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC       are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil bind
CC       in the Q(B) binding site and block subsequent electron transfer.
CC       {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000255|HAMAP-Rule:MF_01379}.
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DR   EMBL; EF067921; ABK20797.1; -; Genomic_DNA.
DR   EMBL; EF067921; ABK20843.1; -; Genomic_DNA.
DR   RefSeq; YP_874574.1; NC_008589.1.
DR   RefSeq; YP_874620.1; NC_008589.1.
DR   PDB; 8IWH; EM; 2.68 A; A/a=11-343.
DR   PDBsum; 8IWH; -.
DR   AlphaFoldDB; A0T0W2; -.
DR   EMDB; EMD-35766; -.
DR   SMR; A0T0W2; -.
DR   STRING; 35128.A0T0W2; -.
DR   GeneID; 4524822; -.
DR   GeneID; 4524891; -.
DR   InParanoid; A0T0W2; -.
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: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:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   CDD; cd09289; Photosystem-II_D1; 1.
DR   Gene3D; 1.20.85.10; Photosystem II protein D1-like; 1.
DR   HAMAP; MF_01379; PSII_PsbA_D1; 1.
DR   InterPro; IPR036854; Photo_II_D1/D2_sf.
DR   InterPro; IPR000484; Photo_RC_L/M.
DR   InterPro; IPR005867; PSII_D1.
DR   NCBIfam; TIGR01151; psbA; 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   1: Evidence at protein level;
KW   3D-structure; Calcium; Chlorophyll; Chloroplast; Chromophore;
KW   Electron transport; Herbicide resistance; Iron; Magnesium; Manganese;
KW   Membrane; Metal-binding; Oxidoreductase; Photosynthesis; Photosystem II;
KW   Plastid; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..344
FT                   /note="Photosystem II protein D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000316521"
FT   PROPEP          345..360
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000316522"
FT   TRANSMEM        29..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        118..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        142..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        197..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        274..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         118
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="ChlzD1"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         126
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         170
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         189
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         198
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="PD1"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         215
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
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_01379"
FT   BINDING         264..265
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         272
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_01379"
FT   BINDING         332
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         333
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         342
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         344
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            161
FT                   /note="Tyrosine radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            190
FT                   /note="Stabilizes free radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            344..345
FT                   /note="Cleavage; by CTPA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
SQ   SEQUENCE   360 AA;  39699 MW;  1274B0B0A53057DD CRC64;
     MIATLERREG VSLWERFCAW ITSTENRLYI GWFGCLMFPT LLTATSCFII AFIAAPPVDI
     DGIREPVAGS LLYGNNIISG AVIPSSNAIG MHFYPIWEAA SVDEWLYNGG PYQLIVLHFL
     LGVASYMGRE WELSYRLGMR PWIFVAFSAP VAAASAVFLV YPIGQGSFSD GMPLGISGTF
     NFMLVFQAEH NILMHPFHMA GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESTNYGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRA LHFFLALWPV LGIWLTAMGI STMAFNLNGF
     NFNQSVVDSQ GRVINTWADI INRADLGMEV MHERNAHNFP LDLASGDVLP VAFTAPAVNA
//