(data stored in SCRATCH3701 zone)

SWISSPROT: PSBA1_SYNS3

ID   PSBA1_SYNS3             Reviewed;         359 AA.
AC   Q0I7J2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 96.
DE   RecName: Full=Photosystem II protein D1 1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE            Short=PSII D1 protein 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE   Flags: Precursor;
GN   Name=psbA1 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305};
GN   OrderedLocusNames=sync_0368;
GN   and
GN   Name=psbA4 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305};
GN   OrderedLocusNames=sync_2384;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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: Cyanobacterial PSII is composed of 1 copy each of membrane
CC       proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC       PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC       proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC       dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01379}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       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: Cyanobacteria usually contain more than 2 copies of the
CC       psbA gene. {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}.
DR   EMBL; CP000435; ABI46731.1; -; Genomic_DNA.
DR   EMBL; CP000435; ABI47825.1; -; Genomic_DNA.
DR   RefSeq; WP_011618340.1; NC_008319.1.
DR   SMR; Q0I7J2; -.
DR   STRING; 64471.sync_1856; -.
DR   EnsemblBacteria; ABI46731; ABI46731; sync_0368.
DR   EnsemblBacteria; ABI47825; ABI47825; sync_2384.
DR   KEGG; syg:sync_0368; -.
DR   KEGG; syg:sync_2384; -.
DR   eggNOG; ENOG4105EY5; Bacteria.
DR   eggNOG; ENOG410XPX5; LUCA.
DR   HOGENOM; HOG000246913; -.
DR   KO; K02703; -.
DR   OrthoDB; 382342at2; -.
DR   BioCyc; SSP64471:G1G72-2211-MONOMER; -.
DR   BioCyc; SSP64471:G1G72-357-MONOMER; -.
DR   Proteomes; UP000001961; Chromosome.
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:0042651; C: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:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
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   PRINTS; PR00256; REACTNCENTRE.
DR   SUPFAM; SSF81483; SSF81483; 1.
DR   TIGRFAMs; TIGR01151; psbA; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0I7J2.
DR   SWISS-2DPAGE; Q0I7J2.
KW   Calcium; Chlorophyll; Chromophore; Electron transport;
KW   Herbicide resistance; Iron; Magnesium; Manganese; Membrane; Metal-binding;
KW   Oxidoreductase; Photosynthesis; Photosystem II; Reference proteome;
KW   Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..344
FT                   /note="Photosystem II protein D1 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000316386"
FT   PROPEP          345..359
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000316387"
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   REGION          264..265
FT                   /note="Quinone (B)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           118
FT                   /note="Magnesium (chlorophyll-a ChlzD1 axial ligand); via
FT                   tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           170
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           170
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           189
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           198
FT                   /note="Magnesium (chlorophyll-a PD1 axial ligand); via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           215
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           272
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           332
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1;
FT                   via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           333
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           333
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           342
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           342
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           344
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via
FT                   carboxylate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           344
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2;
FT                   via carboxylate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         126
FT                   /note="Pheophytin D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         215
FT                   /note="Quinone (B)"
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   359 AA;  39419 MW;  C5D2D5CEC03F0D37 CRC64;
     MTTTIQQRSG ANGWQQFCDW VTSTNNRLYV GWFGVLMIPT LLAATTCFIV AFIAAPPVDI
     DGIREPVAGS LMYGNNIISG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PFQLVVFHFL
     IGIYAYMGRE WELSYRLGMR PWICVAYSAP VAAASAVFLV YPFGQGSFSD AMPLGISGTF
     NYMLVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLVRETTET ESQNYGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGV STMAFNLNGF
     NFNQSILDGQ GRVLNTWADV LNRAGLGMEV MHERNAHNFP LDLAAAESTP VALQAPAIG
//

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