PSBD_BPSYR
ID PSBD_BPSYR Reviewed; 351 AA.
AC Q6H956;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Photosystem II D2 protein;
DE Short=PSII D2 protein;
DE EC=1.10.3.9;
DE AltName: Full=Photosystem Q(A) protein;
GN Name=psbD;
OS Synechococcus phage S-RSM2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae.
OX NCBI_TaxID=264653;
OH NCBI_TaxID=1129; Synechococcus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15263091; DOI=10.1073/pnas.0401478101;
RA Millard A., Clokie M.R., Shub D.A., Mann N.H.;
RT "Genetic organization of the psbAD region in phages infecting marine
RT Synechococcus strains.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11007-11012(2004).
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. D2 is needed for assembly of a stable
CC PSII complex. {ECO:0000250|UniProtKB:D0VWR8}.
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:0000250|UniProtKB:D0VWR8};
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:0000250|UniProtKB:D0VWR8};
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:0000250|UniProtKB:D0VWR8}.
CC -!- SUBCELLULAR LOCATION: Host cellular thylakoid membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000250|UniProtKB:D0VWR8}.
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DR EMBL; AJ628768; CAF32256.1; -; Genomic_DNA.
DR SMR; Q6H956; -.
DR GO; GO:0044160; C:host 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-KW.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR Gene3D; 1.20.85.10; -; 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 PANTHER; PTHR33149; PTHR33149; 1.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; SSF81483; 1.
DR TIGRFAMs; TIGR01152; psbD; 1.
PE 3: Inferred from homology;
KW Chlorophyll; Chromophore; Electron transport; Host membrane;
KW Host thylakoid; Iron; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW Photosynthesis; Photosystem II; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..351
FT /note="Photosystem II D2 protein"
FT /id="PRO_0000359711"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT TRANSMEM 123..139
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT TRANSMEM 151..164
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT TRANSMEM 277..293
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 116
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:0000250|UniProtKB:D0VWR8"
FT BINDING 128
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D2"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 141
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D2"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 196
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:0000250|UniProtKB:D0VWR8"
FT BINDING 213
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="Q(A)"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 260
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="Q(A)"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
SQ SEQUENCE 351 AA; 39351 MW; 0393D4C2950E8207 CRC64;
MVASNLTLQQ RGWFDVLDDW LKRDRFVFVG WSGLLLFPTA YLAIGGWLTG TTFVTSWYTH
GLASSYLEGA NFLTAAVSTP ADAMGHSLLL LWGPEAQGDF IRWCQLGGLW AFVALHGAFA
LIGFMLRQFE LARLIGIRPY NAIAFSGPIA VFVSVFLIYP LGQSSWFFAP SFGVAAIFRF
LLFLQGFHNW TLNPFHMMGV AGILGGALLS AIHGVTVENT LYQDGEQANT FKAFDSTQEE
ETYSMVTANR FWSQIFGIAF SNKRWLHFFM LFVPVMGLWT SSIGIIGLAL NLRAYDFVSQ
EIRASEDPEF ETFYTKNILL NEGLRAWLAP VDQPHENFVF PEEVLPRGNA L
