GENTAUR Molecular Products.

 H2FAE5_9ASPA            Unreviewed;       353 AA.
 H2FAE5;
 21-MAR-2012, integrated into UniProtKB/TrEMBL.
 21-MAR-2012, sequence version 1.
 28-MAR-2018, entry version 39.
 RecName: Full=Photosystem II D2 protein {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004333};
          Short=PSII D2 protein {ECO:0000256|HAMAP-Rule:MF_01383};
          EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01383};
 AltName: Full=Photosystem Q(A) protein {ECO:0000256|HAMAP-Rule:MF_01383};
 Name=psbD {ECO:0000256|HAMAP-Rule:MF_01383,
 ECO:0000313|EMBL:AEX95628.1};
 Hosta ventricosa (blue plantain lily).
 Plastid {ECO:0000313|EMBL:AEX95628.1}.
 Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
 Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
 Agavoideae; Hosta.
 NCBI_TaxID=39527 {ECO:0000313|EMBL:AEX95628.1};
 [1] {ECO:0000313|EMBL:AFA27470.1}
 NUCLEOTIDE SEQUENCE.
 Givnish T.J., Ames M., McNeal J.R., McKain M.J., Steele P.R.,
 dePamphilis C.W., Graham S.W., Pires J.C., Stevenson D.W.,
 Zomlefer W.B., Briggs B.G., Duvall M.R., Moore M.J., Heaney J.M.,
 Soltis D.E., Soltis P.S., Thiele K., Leebens-Mack J.H.;
 "Assembling the Tree of the Monocotyledons: Plastome Sequence
 Phylogeny and Evolution of Poales.";
 Ann. Mo. Bot. Gard. 97:584-616(2010).
 [2] {ECO:0000313|EMBL:AEX95628.1}
 NUCLEOTIDE SEQUENCE.
 PubMed=22291168; DOI=10.3732/ajb.1100491;
 Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
 Pires J.C.;
 "Quality and quantity of data recovered from massively parallel
 sequencing: Examples in Asparagales and Poaceae.";
 Am. J. Bot. 99:330-348(2012).
 [3] {ECO:0000313|EMBL:APO12217.1}
 NUCLEOTIDE SEQUENCE.
 PubMed=27793858;
 McKain M.R., McNeal J.R., Kellar P.R., Eguiarte L.E., Pires J.C.,
 Leebens-Mack J.;
 "Timing of rapid diversification and convergent origins of active
 pollination within Agavoideae (Asparagaceae).";
 Am. J. Bot. 103:1717-1729(2016).
 -!- FUNCTION: Photosystem II (PSII) is a light-driven water:
     plastoquinone oxidoreductase that uses light energy to abstract
     electrons from H(2)O, generating O(2) and a proton gradient
     subsequently used for ATP formation. It consists of a core antenna
     complex that captures photons, and an electron transfer chain that
     converts photonic excitation into a charge separation. The D1/D2
     (PsbA/PsbA) reaction center heterodimer binds P680, the primary
     electron donor of PSII as well as several subsequent electron
     acceptors. D2 is needed for assembly of a stable PSII complex.
     {ECO:0000256|HAMAP-Rule:MF_01383}.
 -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2
     plastoquinol. {ECO:0000256|HAMAP-Rule:MF_01383}.
 -!- COFACTOR:
     Note=The D1/D2 heterodimer binds P680, chlorophylls that are the
     primary electron donor of PSII, and subsequent electron acceptors.
     It shares a non-heme iron and each subunit binds pheophytin,
     quinone, additional chlorophylls, carotenoids and lipids. There is
     also a Cl(-1) ion associated with D1 and D2, which is required for
     oxygen evolution. The PSII complex binds additional chlorophylls,
     carotenoids and specific lipids. {ECO:0000256|HAMAP-
     Rule:MF_01383};
 -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins
     PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL,
     PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
     proteins of the oxygen-evolving complex and a large number of
     cofactors. It forms dimeric complexes. {ECO:0000256|HAMAP-
     Rule:MF_01383}.
 -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
     {ECO:0000256|HAMAP-Rule:MF_01383}; Multi-pass membrane protein
     {ECO:0000256|HAMAP-Rule:MF_01383}.
 -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and
     ChlD2) are entirely coordinated by water. {ECO:0000256|HAMAP-
     Rule:MF_01383}.
 -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
     {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004331}.
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 EMBL; JQ275799; AEX95628.1; -; Genomic_DNA.
 EMBL; HQ181963; AFA27470.1; -; Genomic_DNA.
 EMBL; KX931460; APO12217.1; -; Genomic_DNA.
 RefSeq; YP_009335159.1; NC_032706.1.
 ProteinModelPortal; H2FAE5; -.
 GeneID; 30766911; -.
 GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
 GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
 GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
 GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
 GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
 GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
 GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
 CDD; cd09288; Photosystem-II_D2; 1.
 Gene3D; 1.20.85.10; -; 1.
 HAMAP; MF_01383; PSII_PsbD_D2; 1.
 InterPro; IPR036854; Photo_II_D1/D2_sf.
 InterPro; IPR000484; Photo_RC_L/M.
 InterPro; IPR005868; PSII_PsbD/D2.
 PANTHER; PTHR33149; PTHR33149; 1.
 Pfam; PF00124; Photo_RC; 1.
 PRINTS; PR00256; REACTNCENTRE.
 SUPFAM; SSF81483; SSF81483; 1.
 TIGRFAMs; TIGR01152; psbD; 1.
 PROSITE; PS00244; REACTION_CENTER; 1.
 3: Inferred from homology;
 Chlorophyll {ECO:0000256|HAMAP-Rule:MF_01383};
 Chloroplast {ECO:0000313|EMBL:AEX95628.1};
 Chromophore {ECO:0000256|HAMAP-Rule:MF_01383};
 Electron transport {ECO:0000256|HAMAP-Rule:MF_01383,
 ECO:0000256|RuleBase:RU004333};
 Iron {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004333};
 Magnesium {ECO:0000256|HAMAP-Rule:MF_01383};
 Membrane {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|SAM:Phobius};
 Metal-binding {ECO:0000256|HAMAP-Rule:MF_01383,
 ECO:0000256|RuleBase:RU004333};
 Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01383};
 Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01383,
 ECO:0000256|RuleBase:RU004333};
 Photosystem II {ECO:0000256|HAMAP-Rule:MF_01383,
 ECO:0000256|RuleBase:RU004333}; Plastid {ECO:0000313|EMBL:AEX95628.1};
 Thylakoid {ECO:0000256|HAMAP-Rule:MF_01383};
 Transmembrane {ECO:0000256|HAMAP-Rule:MF_01383,
 ECO:0000256|SAM:Phobius};
 Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01383,
 ECO:0000256|SAM:Phobius};
 Transport {ECO:0000256|HAMAP-Rule:MF_01383,
 ECO:0000256|RuleBase:RU004333}.
 TRANSMEM     28     50       Helical. {ECO:0000256|SAM:Phobius}.
 TRANSMEM    111    129       Helical. {ECO:0000256|SAM:Phobius}.
 TRANSMEM    141    161       Helical. {ECO:0000256|SAM:Phobius}.
 TRANSMEM    167    185       Helical. {ECO:0000256|SAM:Phobius}.
 TRANSMEM    197    217       Helical. {ECO:0000256|SAM:Phobius}.
 TRANSMEM    267    292       Helical. {ECO:0000256|SAM:Phobius}.
 METAL       118    118       Magnesium (chlorophyll-a ChlzD2, axial
                              ligand; peripheral); via tele nitrogen.
                              {ECO:0000256|HAMAP-Rule:MF_01383}.
 METAL       198    198       Magnesium (chlorophyll-a PD2 axial
                              ligand); via tele nitrogen.
                              {ECO:0000256|HAMAP-Rule:MF_01383}.
 METAL       215    215       Iron; shared with heterodimeric partner;
                              via tele nitrogen. {ECO:0000256|HAMAP-
                              Rule:MF_01383}.
 METAL       269    269       Iron; shared with heterodimeric partner;
                              via tele nitrogen. {ECO:0000256|HAMAP-
                              Rule:MF_01383}.
 BINDING     130    130       Pheophytin D2. {ECO:0000256|HAMAP-
                              Rule:MF_01383}.
 BINDING     143    143       Pheophytin D2. {ECO:0000256|HAMAP-
                              Rule:MF_01383}.
 BINDING     215    215       Plastoquinone Q(A). {ECO:0000256|HAMAP-
                              Rule:MF_01383}.
 BINDING     262    262       Plastoquinone Q(A); via amide nitrogen.
                              {ECO:0000256|HAMAP-Rule:MF_01383}.
 NON_TER     353    353       {ECO:0000313|EMBL:AFA27470.1}.
 SEQUENCE   353 AA;  39533 MW;  931633AB4DD25D34 CRC64;
 MTIALGKFAK EENDLFDIMD DWLRRDRFVF VGWSGLLLFP CAYFALGGWF TGTTFVTSWY
 THGLASSYLE GCNFLTAAVS TPANSLAHSL LLLWGPEAQG DFTRWCQLGG LWTFVALHGA
 FGLIGFMLRQ FELARSVQLR PYNAIAFSGP IAVFVSVFLI YPLGQSGWFF APSFGVAAIF
 RFILFFQGFH NWTLNPFHMM GVAGVLGAAL LCAIHGATVE NTLFEDGDGA NTFRAFNPTQ
 AEETYSMVTA NRFWSQIFGV AFSNKRWLHF FMLFVPVTGL WMSALGVVGL ALNLRAYDFV
 SQEIRAAEDP EFETFYTKNI LLNEGIRAWM AAQDQPHENL IFPEEVLPRG NAL

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