(data stored in ACNUC27125 zone)

SWISSPROT: PSBA1_ACAM1

ID   PSBA1_ACAM1             Reviewed;         363 AA.
AC   B0CB14;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 73.
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:0000305}; OrderedLocusNames=AM1_0448;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017;
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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-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   -!- 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}.
CC   -!- CAUTION: This copy of psbA is missing some conserved residues important
CC       for binding the Mn4-Ca-O5 cluster. {ECO:0000305}.
DR   EMBL; CP000828; ABW25504.1; -; Genomic_DNA.
DR   RefSeq; WP_012161111.1; NC_009925.1.
DR   SMR; B0CB14; -.
DR   STRING; 329726.AM1_0448; -.
DR   EnsemblBacteria; ABW25504; ABW25504; AM1_0448.
DR   KEGG; amr:AM1_0448; -.
DR   eggNOG; ENOG4108NSV; Bacteria.
DR   eggNOG; ENOG4110SA6; LUCA.
DR   HOGENOM; HOG000246913; -.
DR   KO; K02703; -.
DR   OMA; HFLIGIW; -.
DR   OrthoDB; 586809at2; -.
DR   Proteomes; UP000000268; 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   PROSITE; PS00244; REACTION_CENTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; B0CB14.
DR   SWISS-2DPAGE; B0CB14.
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..348
FT                   /note="Photosystem II protein D1 1"
FT                   /id="PRO_0000339919"
FT   PROPEP          349..363
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000339920"
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        278..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   REGION          268..269
FT                   /note="Quinone (B)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           121
FT                   /note="Magnesium (chlorophyll-a ChlzD1 axial ligand); via
FT                   tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           173
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           173
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           192
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           201
FT                   /note="Magnesium (chlorophyll-a PD1 axial ligand); via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           218
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           276
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           336
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1;
FT                   via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           348
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via
FT                   carboxylate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   METAL           348
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2;
FT                   via carboxylate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         129
FT                   /note="Pheophytin D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         218
FT                   /note="Quinone (B)"
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"
FT   SITE            348..349
FT                   /note="Cleavage; by CtpA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
SQ   SEQUENCE   363 AA;  39721 MW;  91EA25A2BDE1BFDF CRC64;
     MSTTFQTPSR LPTVSAWDQF CEWITSTHNR LYVGWFGLLM IPSLFVSAIT FMLAWVAAPS
     VDMEGIREPI ISSLLGGSNV ITAAVIPTSA AIGLHLYPLW EATSMDEWLY NGGPYQLIIL
     HFLIAIWTYL GRQWELSYRL GMRPWIAMAF SAPVAAATAV LLVYPMGQGS FSEGLPLGIS
     GTFHFMMAVQ AEHNILMHPF HMLGVVGVFG GAFLSAMHGS LVTSSLVQET SSLKSVNTGY
     KFGQQEATYN LLAGHAGYLG RLFIPDIAFR NSRSIHFLLA VLPTIGIWFA ALGIGTMAFN
     LNGFNFNHSL LDSSGRPIRT EADLLNRATM GLQVMHSVNA HHFSLTLAST ESKEIPTIPI
     MTS
//

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