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Database: UniProt
Entry: A3YVS8_9SYNE
LinkDB: A3YVS8_9SYNE
Original site: A3YVS8_9SYNE 
ID   A3YVS8_9SYNE            Unreviewed;       359 AA.
AC   A3YVS8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379};
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   ORFNames=WH5701_01120 {ECO:0000313|EMBL:EAQ75406.1}, WH5701_10719
GN   {ECO:0000313|EMBL:EAQ73803.1}, WH5701_15526
GN   {ECO:0000313|EMBL:EAQ76230.1};
OS   Synechococcus sp. WH 5701.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=69042 {ECO:0000313|EMBL:EAQ76230.1, ECO:0000313|Proteomes:UP000002935};
RN   [1] {ECO:0000313|EMBL:EAQ76230.1, ECO:0000313|Proteomes:UP000002935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 5701 {ECO:0000313|EMBL:EAQ76230.1}, and WH5701
RC   {ECO:0000313|Proteomes:UP000002935};
RA   Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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/PsbD) reaction center heterodimer
CC       binds P680, the primary electron donor of PSII as well as several
CC       subsequent electron acceptors. {ECO:0000256|ARBA:ARBA00037683,
CC       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   -!- 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, peripheral proteins PsbO, CyanoQ (PsbQ),
CC       PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000256|HAMAP-Rule:MF_01379}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000256|ARBA:ARBA00004636, ECO:0000256|HAMAP-Rule:MF_01379};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004636,
CC       ECO:0000256|HAMAP-Rule:MF_01379}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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: Cyanobacteriota usually contain more than 2 copies of
CC       the psbA gene. {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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAQ76230.1}.
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DR   EMBL; AANO01000013; EAQ73803.1; -; Genomic_DNA.
DR   EMBL; AANO01000004; EAQ75406.1; -; Genomic_DNA.
DR   EMBL; AANO01000002; EAQ76230.1; -; Genomic_DNA.
DR   RefSeq; WP_006170931.1; NZ_CH724160.1.
DR   AlphaFoldDB; A3YVS8; -.
DR   eggNOG; ENOG502Z87P; Bacteria.
DR   HOGENOM; CLU_054206_1_0_3; -.
DR   OrthoDB; 505356at2; -.
DR   Proteomes; UP000002935; Unassembled WGS sequence.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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; 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:SF12; PHOTOSYSTEM II D2 PROTEIN; 1.
DR   PANTHER; PTHR33149; 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   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|HAMAP-Rule:MF_01379};
KW   Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP-
KW   Rule:MF_01379};
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP-
KW   Rule:MF_01379}; Electron transport {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Herbicide resistance {ECO:0000256|ARBA:ARBA00022646, ECO:0000256|HAMAP-
KW   Rule:MF_01379}; Iron {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   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_01379}; Photosystem II {ECO:0000256|HAMAP-Rule:MF_01379};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002935};
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}; Transport {ECO:0000256|HAMAP-Rule:MF_01379}.
FT   CHAIN           1..344
FT                   /note="Photosystem II protein D1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT                   /id="PRO_5034767605"
FT   PROPEP          345..359
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT                   /id="PRO_5034767604"
FT   TRANSMEM        29..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..161
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"
SQ   SEQUENCE   359 AA;  39389 MW;  F17020730CF7A7BA CRC64;
     MTTTLQQRQG ASAWSQFCEW VTSTNNRLYV GWFGVLMIPT LLAATICFIV AFVAAPPVDI
     DGIREPVAGS LLYGNNIISG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLVIFHFL
     IGIFCYMGRE WELSYRLGMR PWICVAYSAP VAAASAVFLI YPFGQGSFSD GMPLGISGTF
     NFMLVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLVRETTES ESQNYGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGV STMAFNLNGF
     NFNQSILDGQ GRVINTWADV LNRAGLGMEV MHERNAHNFP LDLASAEATP VALTAPAIG
//
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