ID   A0A0A0QF08_9MARC        Unreviewed;       353 AA.
AC   A0A0A0QF08;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   12-OCT-2022, entry version 29.
DE   RecName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004332};
DE            Short=PSII D1 protein {ECO:0000256|HAMAP-Rule:MF_01379};
DE            EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01379};
DE   AltName: Full=Photosystem II Q(B) protein {ECO:0000256|HAMAP-Rule:MF_01379};
GN   Name=psbA {ECO:0000256|HAMAP-Rule:MF_01379,
GN   ECO:0000313|EMBL:AII83374.1};
OS   Isotachis stephanii.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AII83374.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Jungermanniopsida; Jungermanniidae; Jungermanniales; Jungermanniineae;
OC   Balantiopsidaceae; Isotachis.
OX   NCBI_TaxID=1527735 {ECO:0000313|EMBL:AII83374.1};
RN   [1] {ECO:0000313|EMBL:AII83374.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FATOL790 {ECO:0000313|EMBL:AII83374.1};
RA   Laenen B., Shaw B., Desamore A., Paradis E., Schneider H., Heinrichs J.,
RA   Villarreal J.C., Gradstein R., McDaniel S., Long D., Forrest L.,
RA   Crandall-Stotler B., Stotler R., Davis C., Engel J., Von Konrat M.,
RA   Vanderpoorten A., Shaw J.;
RT   "Old but still active: liverworts (Marchantiophyta) are not a sphinx of the
RT   past.";
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. {ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01379}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid,
CC       chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01379};
CC       Multi-pass membrane protein {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01379}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC       are entirely coordinated by water. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01379}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000256|ARBA:ARBA00008204, ECO:0000256|HAMAP-Rule:MF_01379,
CC       ECO:0000256|RuleBase:RU004331}.
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DR   EMBL; KF851892; AII83374.1; -; Genomic_DNA.
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:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC.
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; -; 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   PRINTS; PR00256; REACTNCENTRE.
DR   SUPFAM; SSF81483; SSF81483; 1.
DR   TIGRFAMs; TIGR01151; psbA; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|HAMAP-Rule:MF_01379};
KW   Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP-
KW   Rule:MF_01379}; Chloroplast {ECO:0000313|EMBL:AII83374.1};
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP-
KW   Rule:MF_01379};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_01379};
KW   Herbicide resistance {ECO:0000256|ARBA:ARBA00022646, ECO:0000256|HAMAP-
KW   Rule:MF_01379};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01379};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01379};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01379};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01379};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01379}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_01379};
KW   Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW   Rule:MF_01379}; Plastid {ECO:0000313|EMBL:AII83374.1};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01379};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01379};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01379}.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   CHAIN           2..344
FT                   /note="Photosystem II protein D1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT                   /id="PRO_5023454678"
FT   PROPEP          345..353
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT                   /id="PRO_5007332470"
FT   TRANSMEM        29..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..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..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
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:0000256|HAMAP-Rule:MF_01379"
FT   BINDING         126
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   BINDING         170
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   BINDING         189
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01379"
FT   BINDING         215
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01379"
FT   BINDING         332
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   BINDING         333
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   BINDING         342
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   BINDING         344
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   SITE            161
FT                   /note="Tyrosine radical intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   SITE            190
FT                   /note="Stabilizes free radical intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   SITE            344..345
FT                   /note="Cleavage; by CtpA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT   MOD_RES         2
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
SQ   SEQUENCE   353 AA;  38807 MW;  7623F31378D965BD CRC64;
     MTATLERRES ASIWGRFCDW ITSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI
     DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL
     LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF
     NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANAGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF
     NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAAIEAPV TNG
//