位置:首页 > 蛋白库 > PSBD_NUPAD
PSBD_NUPAD
ID   PSBD_NUPAD              Reviewed;         353 AA.
AC   Q4FFP2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 76.
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};
DE   AltName: Full=Photosystem Q(A) protein {ECO:0000255|HAMAP-Rule:MF_01383};
GN   Name=psbD {ECO:0000255|HAMAP-Rule:MF_01383};
OS   Nuphar advena (Common spatterdock) (Nuphar lutea subsp. advena).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Nymphaeales; Nymphaeaceae; Nuphar.
OX   NCBI_TaxID=77108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15944438; DOI=10.1093/molbev/msi191;
RA   Leebens-Mack J., Raubeson L.A., Cui L., Kuehl J.V., Fourcade M.H.,
RA   Chumley T.W., Boore J.L., Jansen R.K., dePamphilis C.W.;
RT   "Identifying the basal angiosperm node in chloroplast genome phylogenies:
RT   sampling one's way out of the Felsenstein zone.";
RL   Mol. Biol. Evol. 22:1948-1963(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17573971; DOI=10.1186/1471-2164-8-174;
RA   Raubeson L.A., Peery R., Chumley T.W., Dziubek C., Fourcade H.M.,
RA   Boore J.L., Jansen R.K.;
RT   "Comparative chloroplast genomics: analyses including new sequences from
RT   the angiosperms Nuphar advena and Ranunculus macranthus.";
RL   BMC Genomics 8:174-174(2007).
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   -!- 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   -!- 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       The PSII complex binds additional chlorophylls, carotenoids and
CC       specific lipids. {ECO:0000255|HAMAP-Rule:MF_01383};
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC       PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC       PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC       evolving complex and a large number of cofactors. It forms dimeric
CC       complexes. {ECO:0000255|HAMAP-Rule:MF_01383}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01383}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01383}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC       are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01383}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000255|HAMAP-Rule:MF_01383}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ069639; AAZ04071.1; -; Genomic_DNA.
DR   EMBL; DQ354691; ABC60453.1; -; Genomic_DNA.
DR   RefSeq; YP_001001529.1; NC_008788.1.
DR   AlphaFoldDB; Q4FFP2; -.
DR   SMR; Q4FFP2; -.
DR   GeneID; 4699580; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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   3: Inferred from homology;
KW   Acetylation; Chlorophyll; Chloroplast; Chromophore; Electron transport;
KW   Iron; Magnesium; Membrane; Metal-binding; Oxidoreductase; Phosphoprotein;
KW   Photosynthesis; Photosystem II; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P56761"
FT   CHAIN           2..353
FT                   /note="Photosystem II D2 protein"
FT                   /id="PRO_0000359673"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        125..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        153..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   TRANSMEM        279..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         118
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   BINDING         130
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         143
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         198
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   BINDING         215
FT                   /ligand="a plastoquinone"
FT                   /ligand_id="ChEBI:CHEBI:17757"
FT                   /ligand_label="Q(A)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         215
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   BINDING         262
FT                   /ligand="a plastoquinone"
FT                   /ligand_id="ChEBI:CHEBI:17757"
FT                   /ligand_label="Q(A)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01383"
FT   BINDING         269
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   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P56761"
FT   MOD_RES         2
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P56761"
SQ   SEQUENCE   353 AA;  39606 MW;  9673AE32B7C976B5 CRC64;
     MTIALGRFTK EENDLFDIMD DWLRRDRFVF VGWSGLLLFP CAYFALGGWF TGTTFVTSWY
     THGLASSYLE GCNFLTAAVS TPANSLAHSL LLLWGPEAQG DFTRWCQLGG LWTFVALHGA
     FGLIGFMLRQ FELARSVQLR PYNAIAFSAP IAVFVSVFLI YPLGQSGWFF APSFGVAAIF
     RFILFFQGFH NWTLNPFHMM GVAGVLGAAL LCAIHGATVE NTLFEDGDGA NTFRAFNPTQ
     AEETYSMVTA NRFWSQIFGV AFSNKRWLHF FMLFVPVTGL WMSALGVVGL ALNLRAYDFV
     SQEIRAAEDP EFETFYTKNI LLNEGIRAWM AAQDQPHENL IFPEEVLPRG NAL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024