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Database: UniProt
Entry: Q8CM25
LinkDB: Q8CM25
Original site: Q8CM25 
ID   PSBD_THEEB              Reviewed;         352 AA.
AC   Q8CM25;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   02-DEC-2020, entry version 122.
DE   RecName: Full=Photosystem II D2 protein {ECO:0000255|HAMAP-Rule:MF_01383};
DE            Short=PSII D2 protein {ECO:0000255|HAMAP-Rule:MF_01383};
DE            EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:25006873};
DE   AltName: Full=Photosystem II Q(A) protein {ECO:0000255|HAMAP-Rule:MF_01383};
GN   Name=psbD1 {ECO:0000255|HAMAP-Rule:MF_01383}; OrderedLocusNames=tlr0455;
GN   and
GN   Name=psbD2 {ECO:0000255|HAMAP-Rule:MF_01383}; OrderedLocusNames=tlr1630;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH IRON,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   DOI=10.1039/B406989G;
RA   Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.;
RT   "Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a
RT   closer look at the Mn-cluster.";
RL   Phys. Chem. Chem. Phys. 6:4733-4736(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN PHOTOSYSTEM II WITH IRON,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=14764885; DOI=10.1126/science.1093087;
RA   Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
RT   "Architecture of the photosynthetic oxygen-evolving center.";
RL   Science 303:1831-1838(2004).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN PHOTOSYSTEM II WITH IRON,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=16355230; DOI=10.1038/nature04224;
RA   Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
RT   "Towards complete cofactor arrangement in the 3.0 A resolution structure of
RT   photosystem II.";
RL   Nature 438:1040-1044(2005).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II WITH IRON,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=BP-1;
RX   PubMed=19219048; DOI=10.1038/nsmb.1559;
RA   Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
RT   "Cyanobacterial photosystem II at 2.9-A resolution and the role of
RT   quinones, lipids, channels and chloride.";
RL   Nat. Struct. Mol. Biol. 16:334-342(2009).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II WITH IRON,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA   Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA   Zouni A.;
RT   "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT   elongatus at 3.6 A resolution.";
RL   J. Biol. Chem. 285:26255-26262(2010).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH IRON,
RP   FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=21367867; DOI=10.1074/jbc.m110.215970;
RA   Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J.,
RA   Muh F., Dau H., Saenger W., Zouni A.;
RT   "Structural basis of cyanobacterial photosystem II inhibition by the
RT   herbicide terbutryn.";
RL   J. Biol. Chem. 286:15964-15972(2011).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=22665786; DOI=10.1073/pnas.1204598109;
RA   Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
RA   Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
RA   Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A.,
RA   DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A., Schafer D.W.,
RA   Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D.,
RA   Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Room temperature femtosecond X-ray diffraction of photosystem II
RT   microcrystals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=23413188; DOI=10.1126/science.1234273;
RA   Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
RA   Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B.,
RA   Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D.,
RA   Fry A.R., Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M.,
RA   Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J.,
RA   Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D.,
RA   Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K.,
RA   Yachandra V.K., Bergmann U., Yano J.;
RT   "Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem
RT   II at room temperature.";
RL   Science 340:491-495(2013).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 11-352 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25043005; DOI=10.1038/nature13453;
RA   Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N.,
RA   Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H.,
RA   Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L.,
RA   Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R.,
RA   Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M.,
RA   Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H.,
RA   Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M.,
RA   Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M.,
RA   Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L.,
RA   Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M.,
RA   Chapman H.N., Spence J.C., Fromme P.;
RT   "Serial time-resolved crystallography of photosystem II using a femtosecond
RT   X-ray laser.";
RL   Nature 513:261-265(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25006873; DOI=10.1038/ncomms5371;
RA   Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
RA   Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
RA   Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A.,
RA   Gloeckner C., Lampe A., DiFiore D., Milathianaki D., Fry A.R.,
RA   Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C.,
RA   Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P.,
RA   Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Taking snapshots of photosynthetic water oxidation using femtosecond X-ray
RT   diffraction and spectroscopy.";
RL   Nat. Commun. 5:4371-4371(2014).
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:0000255|HAMAP-Rule:MF_01383,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:25006873}.
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_01383,
CC         ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:25006873};
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       (PubMed:19219048, PubMed:21367867). PSII binds additional chlorophylls,
CC       carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01383,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005, ECO:0000269|Ref.2};
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_01383,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005, ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01383, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
CC       ECO:0000269|Ref.2}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01383, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
CC       ECO:0000269|Ref.2}.
CC   -!- MASS SPECTROMETRY: Mass=39290; Mass_error=79; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC       are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01383,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000255|HAMAP-Rule:MF_01383}.
CC   -!- CAUTION: According to (Ref.2, PubMed:22665786, PubMed:23413188,
CC       PubMed:25006873) there are no direct protein ligands to pheophytin D2,
CC       whereas (PubMed:14764885, PubMed:16355230, PubMed:19219048,
CC       PubMed:20558739, PubMed:21367867, PubMed:25043005) show 1 or 2 direct
CC       ligands. {ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
CC       ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:20558739,
CC       ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:22665786,
CC       ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25006873,
CC       ECO:0000303|PubMed:25043005, ECO:0000303|Ref.2}.
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DR   EMBL; BA000039; BAC08007.1; -; Genomic_DNA.
DR   EMBL; BA000039; BAC09182.1; -; Genomic_DNA.
DR   RefSeq; NP_681245.1; NC_004113.1.
DR   RefSeq; NP_682420.1; NC_004113.1.
DR   RefSeq; WP_011056308.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; D/d=1-352.
DR   PDB; 1W5C; X-ray; 3.20 A; D/J=1-352.
DR   PDB; 2AXT; X-ray; 3.00 A; D/d=1-352.
DR   PDB; 3KZI; X-ray; 3.60 A; D=1-352.
DR   PDB; 4FBY; X-ray; 6.56 A; D/Q=1-352.
DR   PDB; 4IXQ; X-ray; 5.70 A; D/d=1-352.
DR   PDB; 4IXR; X-ray; 5.90 A; D/d=1-352.
DR   PDB; 4PBU; X-ray; 5.00 A; D/d=11-352.
DR   PDB; 4PJ0; X-ray; 2.44 A; D/d=1-352.
DR   PDB; 4RVY; X-ray; 5.50 A; D/d=11-352.
DR   PDB; 4TNH; X-ray; 4.90 A; D/d=1-352.
DR   PDB; 4TNI; X-ray; 4.60 A; D/d=1-352.
DR   PDB; 4TNJ; X-ray; 4.50 A; D/d=1-352.
DR   PDB; 4TNK; X-ray; 5.20 A; D/d=1-352.
DR   PDB; 4V62; X-ray; 2.90 A; AD/BD=1-352.
DR   PDB; 4V82; X-ray; 3.20 A; AD/BD=1-352.
DR   PDB; 5E79; X-ray; 3.50 A; D/d=11-352.
DR   PDB; 5E7C; X-ray; 4.50 A; D/d=11-352.
DR   PDB; 5H2F; X-ray; 2.20 A; D/d=11-352.
DR   PDB; 5KAF; X-ray; 3.00 A; D/d=1-352.
DR   PDB; 5KAI; X-ray; 2.80 A; D/d=1-352.
DR   PDB; 5MX2; X-ray; 2.20 A; D/d=1-352.
DR   PDB; 5TIS; X-ray; 2.25 A; D/d=1-352.
DR   PDB; 5ZZN; X-ray; 2.10 A; D/d=11-352.
DR   PDB; 6DHE; X-ray; 2.05 A; D/d=12-352.
DR   PDB; 6DHF; X-ray; 2.08 A; D/d=12-352.
DR   PDB; 6DHG; X-ray; 2.50 A; D/d=12-352.
DR   PDB; 6DHH; X-ray; 2.20 A; D/d=12-352.
DR   PDB; 6DHO; X-ray; 2.07 A; D/d=12-352.
DR   PDB; 6DHP; X-ray; 2.04 A; D/d=12-352.
DR   PDB; 6W1O; X-ray; 2.08 A; D/d=1-352.
DR   PDB; 6W1P; X-ray; 2.26 A; D/d=1-352.
DR   PDB; 6W1Q; X-ray; 2.27 A; D/d=1-352.
DR   PDB; 6W1R; X-ray; 2.23 A; D/d=1-352.
DR   PDB; 6W1T; X-ray; 2.01 A; D/d=1-352.
DR   PDB; 6W1U; X-ray; 2.09 A; D/d=1-352.
DR   PDB; 6W1V; X-ray; 2.09 A; D/d=1-352.
DR   PDBsum; 1S5L; -.
DR   PDBsum; 1W5C; -.
DR   PDBsum; 2AXT; -.
DR   PDBsum; 3KZI; -.
DR   PDBsum; 4FBY; -.
DR   PDBsum; 4IXQ; -.
DR   PDBsum; 4IXR; -.
DR   PDBsum; 4PBU; -.
DR   PDBsum; 4PJ0; -.
DR   PDBsum; 4RVY; -.
DR   PDBsum; 4TNH; -.
DR   PDBsum; 4TNI; -.
DR   PDBsum; 4TNJ; -.
DR   PDBsum; 4TNK; -.
DR   PDBsum; 4V62; -.
DR   PDBsum; 4V82; -.
DR   PDBsum; 5E79; -.
DR   PDBsum; 5E7C; -.
DR   PDBsum; 5H2F; -.
DR   PDBsum; 5KAF; -.
DR   PDBsum; 5KAI; -.
DR   PDBsum; 5MX2; -.
DR   PDBsum; 5TIS; -.
DR   PDBsum; 5ZZN; -.
DR   PDBsum; 6DHE; -.
DR   PDBsum; 6DHF; -.
DR   PDBsum; 6DHG; -.
DR   PDBsum; 6DHH; -.
DR   PDBsum; 6DHO; -.
DR   PDBsum; 6DHP; -.
DR   PDBsum; 6W1O; -.
DR   PDBsum; 6W1P; -.
DR   PDBsum; 6W1Q; -.
DR   PDBsum; 6W1R; -.
DR   PDBsum; 6W1T; -.
DR   PDBsum; 6W1U; -.
DR   PDBsum; 6W1V; -.
DR   SMR; Q8CM25; -.
DR   DIP; DIP-48490N; -.
DR   IntAct; Q8CM25; 1.
DR   STRING; 197221.22295355; -.
DR   EnsemblBacteria; BAC08007; BAC08007; BAC08007.
DR   EnsemblBacteria; BAC09182; BAC09182; BAC09182.
DR   KEGG; tel:tlr0455; -.
DR   KEGG; tel:tlr1630; -.
DR   PATRIC; fig|197221.4.peg.1710; -.
DR   eggNOG; ENOG502Z8JK; Bacteria.
DR   OMA; QGDFVRW; -.
DR   OrthoDB; 410807at2; -.
DR   BRENDA; 1.10.3.9; 7763.
DR   EvolutionaryTrace; Q8CM25; -.
DR   Proteomes; UP000000440; 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:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   CDD; cd09288; Photosystem-II_D2; 1.
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.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chlorophyll; Chromophore; Electron transport; Iron;
KW   Magnesium; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Photosystem II; Reference proteome; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..352
FT                   /note="Photosystem II D2 protein"
FT                   /id="PRO_0000359603"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        33..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        50..112
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        113..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        128..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        144..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        157..194
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        195..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        214..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        271..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        286..352
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   METAL           117
FT                   /note="Magnesium (chlorophyll-a ChlzD2, axial ligand;
FT                   peripheral); via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:20558739,
FT                   ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:22665786,
FT                   ECO:0000303|PubMed:23413188, ECO:0000303|Ref.2"
FT   METAL           197
FT                   /note="Magnesium (chlorophyll-a PD2 axial ligand); via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:20558739,
FT                   ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:22665786,
FT                   ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25043005,
FT                   ECO:0000303|Ref.2"
FT   METAL           214
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:20558739,
FT                   ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:22665786,
FT                   ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25043005,
FT                   ECO:0000303|Ref.2"
FT   METAL           268
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:20558739,
FT                   ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:22665786,
FT                   ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25006873,
FT                   ECO:0000303|PubMed:25043005, ECO:0000303|Ref.2"
FT   BINDING         129
FT                   /note="Pheophytin D2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383,
FT                   ECO:0000269|PubMed:16355230, ECO:0000303|PubMed:14764885,
FT                   ECO:0000303|PubMed:25043005"
FT   BINDING         142
FT                   /note="Pheophytin D2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:20558739, ECO:0000303|PubMed:21367867,
FT                   ECO:0000303|PubMed:25043005"
FT   BINDING         214
FT                   /note="Plastoquinone Q(A)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:20558739,
FT                   ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:22665786,
FT                   ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25006873,
FT                   ECO:0000303|PubMed:25043005"
FT   BINDING         261
FT                   /note="Plastoquinone Q(A); via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:20558739,
FT                   ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:22665786,
FT                   ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25006873,
FT                   ECO:0000303|PubMed:25043005"
FT   HELIX           14..22
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          26..28
FT                   /evidence="ECO:0000244|PDB:1W5C"
FT   HELIX           31..54
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           58..61
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           67..69
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            73..75
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           83..85
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            95..99
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           101..106
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           109..136
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           141..145
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           147..157
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           159..163
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          164..166
FT                   /evidence="ECO:0000244|PDB:5MX2"
FT   HELIX           167..169
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           175..189
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           191..193
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           195..220
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          221..223
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          224..226
FT                   /evidence="ECO:0000244|PDB:1W5C"
FT   STRAND          227..229
FT                   /evidence="ECO:0000244|PDB:5TIS"
FT   HELIX           231..234
FT                   /evidence="ECO:0000244|PDB:5MX2"
FT   HELIX           246..257
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           264..290
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           299..307
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           314..333
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           335..337
FT                   /evidence="ECO:0000244|PDB:5MX2"
FT   HELIX           343..345
FT                   /evidence="ECO:0000244|PDB:5ZZN"
SQ   SEQUENCE   352 AA;  39361 MW;  C5D91543CD148FD4 CRC64;
     MTIAIGRAPA ERGWFDILDD WLKRDRFVFV GWSGILLFPC AYLALGGWLT GTTFVTSWYT
     HGLASSYLEG CNFLTVAVST PANSMGHSLL LLWGPEAQGD FTRWCQLGGL WTFIALHGAF
     GLIGFMLRQF EIARLVGVRP YNAIAFSAPI AVFVSVFLIY PLGQSSWFFA PSFGVAAIFR
     FLLFFQGFHN WTLNPFHMMG VAGVLGGALL CAIHGATVEN TLFQDGEGAS TFRAFNPTQA
     EETYSMVTAN RFWSQIFGIA FSNKRWLHFF MLFVPVTGLW MSAIGVVGLA LNLRSYDFIS
     QEIRAAEDPE FETFYTKNLL LNEGIRAWMA PQDQPHENFV FPEEVLPRGN AL
//
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