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PSBA_HETNI
ID   PSBA_HETNI              Reviewed;         347 AA.
AC   Q9MSC0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, 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};
GN   Name=psbA {ECO:0000255|HAMAP-Rule:MF_01379};
OS   Heterocapsa niei (Dinoflagellate) (Cachonina niei).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Peridiniales; Heterocapsaceae;
OC   Heterocapsa.
OX   NCBI_TaxID=2920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCMP447;
RX   PubMed=10903370; DOI=10.1007/s002390010064;
RA   Zhang Z., Green B.R., Cavalier-Smith T.;
RT   "Phylogeny of ultra-rapidly evolving dinoflagellate chloroplast genes: a
RT   possible common origin for sporozoan and dinoflagellate plastids.";
RL   J. Mol. Evol. 51:26-40(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCMP447;
RX   PubMed=11919290; DOI=10.1093/oxfordjournals.molbev.a004104;
RA   Zhang Z., Cavalier-Smith T., Green B.R.;
RT   "Evolution of dinoflagellate unigenic minicircles and the partially
RT   concerted divergence of their putative replicon origins.";
RL   Mol. Biol. Evol. 19:489-500(2002).
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. {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, 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_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-164 forms a radical intermediate that is referred to as redox-
CC       active TyrZ, YZ or Y-Z. {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; AF206709; AAF89983.1; -; Genomic_DNA.
DR   EMBL; AY004265; AAG25878.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9MSC0; -.
DR   SMR; Q9MSC0; -.
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: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   Gene3D; 1.20.85.10; -; 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   PANTHER; PTHR33149; PTHR33149; 1.
DR   Pfam; PF00124; Photo_RC; 1.
DR   SUPFAM; SSF81483; SSF81483; 1.
DR   TIGRFAMs; TIGR01151; psbA; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   3: Inferred from homology;
KW   Calcium; Chlorophyll; Chloroplast; Chromophore; Electron transport;
KW   Herbicide resistance; Iron; Magnesium; Manganese; Membrane; Metal-binding;
KW   Oxidoreductase; Photosynthesis; Photosystem II; Plastid; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..347
FT                   /note="Photosystem II protein D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000316496"
FT   TRANSMEM        32..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        121..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        145..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        200..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        277..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         121
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         129
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         173
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         192
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         201
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         218
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         218
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         267..268
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         275
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         335
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         336
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         345
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         347
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            164
FT                   /note="Tyrosine radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            193
FT                   /note="Stabilizes free radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
SQ   SEQUENCE   347 AA;  38026 MW;  56BC47E420FDD002 CRC64;
     MKNTFNTSVF ANAYSFWGYV IGFILSTSNR LYIGWFGILM FPLLVLATVA FISAFIFAPP
     VDIDGIREPV AGALLYGNNI ISGAVIPSSN AIGVHFYPVW EALGFDEWLY NGGTYQFVVL
     HFILGAGAYM GREWEFAFRL GMRPWIFVAF SAPLVAASAV FVVYPIGQGS FSDGMPLGIS
     GTFNFMLVFQ AEHNILMHPF HILGVAAVFG GSLFSAMHGS LVTSSLLAET AGDLSLNVGY
     NFGQEDETYS ISAAHGYFGR LIFQYASFNN SRSLHFFLAA WPVIGIWFTA LGVSTMAFNL
     NGLNFNQSII DSSGHLINSW ADIVNRADLG MEVMHERNAH NFPLDLA
 
 
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