PSBD_THEVB
ID PSBD_THEVB Reviewed; 352 AA.
AC Q8CM25;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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 PDB; 7NHO; EM; 2.66 A; D=1-352.
DR PDB; 7NHP; EM; 2.72 A; D=1-352.
DR PDB; 7NHQ; EM; 2.68 A; D=1-352.
DR PDB; 7RF1; X-ray; 1.89 A; D/d=1-352.
DR PDB; 7RF2; X-ray; 2.08 A; D/d=1-352.
DR PDB; 7RF3; X-ray; 2.26 A; D/d=1-352.
DR PDB; 7RF4; X-ray; 2.27 A; D/d=1-352.
DR PDB; 7RF5; X-ray; 2.23 A; D/d=1-352.
DR PDB; 7RF6; X-ray; 2.01 A; D/d=1-352.
DR PDB; 7RF7; X-ray; 2.09 A; D/d=1-352.
DR PDB; 7RF8; 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 PDBsum; 7NHO; -.
DR PDBsum; 7NHP; -.
DR PDBsum; 7NHQ; -.
DR PDBsum; 7RF1; -.
DR PDBsum; 7RF2; -.
DR PDBsum; 7RF3; -.
DR PDBsum; 7RF4; -.
DR PDBsum; 7RF5; -.
DR PDBsum; 7RF6; -.
DR PDBsum; 7RF7; -.
DR PDBsum; 7RF8; -.
DR AlphaFoldDB; Q8CM25; -.
DR SMR; Q8CM25; -.
DR DIP; DIP-48490N; -.
DR IntAct; Q8CM25; 1.
DR STRING; 197221.22294176; -.
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; RWFQLGG; -.
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: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:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
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 BINDING 117
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: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 BINDING 129
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="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 /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="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 197
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: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 BINDING 214
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="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 214
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
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 BINDING 261
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="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 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
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 HELIX 14..22
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1W5C"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:7NHQ"
FT TURN 95..99
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 109..136
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5MX2"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 175..189
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 195..220
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1W5C"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5TIS"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:5MX2"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:7NHQ"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7NHQ"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 264..290
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 314..333
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5MX2"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:7NHQ"
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
