PSBA_SPIOL
ID PSBA_SPIOL Reviewed; 353 AA.
AC P69560; P02955;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Photosystem II protein D1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE Short=PSII D1 protein {ECO:0000255|HAMAP-Rule:MF_01379};
DE EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379};
DE AltName: Full=32 kDa thylakoid membrane protein {ECO:0000303|PubMed:16593262};
DE AltName: Full=Photosystem II Q(B) protein {ECO:0000255|HAMAP-Rule:MF_01379};
DE Flags: Precursor;
GN Name=psbA {ECO:0000255|HAMAP-Rule:MF_01379};
OS Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16593262; DOI=10.1073/pnas.79.24.7699;
RA Zurawski G., Bohnert H.J., Whitfeld P.R., Bottomley W.;
RT "Nucleotide sequence of the gene for the M-r 32,000 thylakoid membrane
RT protein from Spinacia oleracea and Nicotiana debneyi predicts a totally
RT conserved primary translation product of M-r 38,950.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:7699-7703(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-8, ACETYLATION AT THR-2, AND PHOSPHORYLATION AT
RP THR-2.
RX PubMed=3121625; DOI=10.1016/s0021-9258(19)57275-1;
RA Michel H., Hunt D.F., Shabanowitz J., Bennett J.;
RT "Tandem mass spectrometry reveals that three photosystem II proteins of
RT spinach chloroplasts contain N-acetyl-O-phosphothreonine at their NH2
RT termini.";
RL J. Biol. Chem. 263:1123-1130(1988).
RN [4]
RP PROTEOLYTIC PROCESSING.
RX PubMed=3056748; DOI=10.1016/0014-5793(88)80330-2;
RA Takahashi M., Shiraishi T., Asada K.;
RT "COOH-terminal residues of D1 and the 44 kDa CPa-2 at spinach photosystem
RT II core complex.";
RL FEBS Lett. 240:6-8(1988).
RN [5]
RP MASS SPECTROMETRY.
RX PubMed=9655347; DOI=10.1002/pro.5560070619;
RA Whitelegge J.P., Gundersen C.B., Faull K.F.;
RT "Electrospray-ionization mass spectrometry of intact intrinsic membrane
RT proteins.";
RL Protein Sci. 7:1423-1430(1998).
RN [6]
RP 3D-STRUCTURE MODELING.
RX PubMed=8931545; DOI=10.1021/bi960764k;
RA Svensson B., Etchebest C., Tuffery P., van Kan P., Smith J., Styring S.;
RT "A model for the photosystem II reaction center core including the
RT structure of the primary donor P680.";
RL Biochemistry 35:14486-14502(1996).
CC -!- FUNCTION: This is one of the two reaction center proteins of
CC photosystem II.
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: 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_01379}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01379}.
CC -!- PTM: Tyr-161 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 -!- MASS SPECTROMETRY: Mass=38022.1; Mass_error=3.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9655347};
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}.
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DR EMBL; AJ400848; CAB88705.1; -; Genomic_DNA.
DR PIR; A38055; FMSP32.
DR RefSeq; NP_054912.1; NC_002202.1.
DR PDB; 3JCU; EM; 3.20 A; A/a=1-344.
DR PDBsum; 3JCU; -.
DR AlphaFoldDB; P69560; -.
DR SMR; P69560; -.
DR DIP; DIP-62007N; -.
DR IntAct; P69560; 1.
DR STRING; 3562.P69560; -.
DR BindingDB; P69560; -.
DR ChEMBL; CHEMBL2366481; -.
DR CarbonylDB; P69560; -.
DR iPTMnet; P69560; -.
DR GeneID; 2715607; -.
DR KEGG; soe:2715607; -.
DR OrthoDB; 801765at2759; -.
DR PRO; PR:P69560; -.
DR Proteomes; UP000054095; Chloroplast.
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; IBA:GO_Central.
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:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR CDD; cd09289; Photosystem-II_D1; 1.
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 TIGRFAMs; TIGR01151; psbA; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Chlorophyll; Chloroplast; Chromophore;
KW Direct protein sequencing; Electron transport; Herbicide resistance; Iron;
KW Magnesium; Manganese; Membrane; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3121625"
FT CHAIN 2..344
FT /note="Photosystem II protein D1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000030246"
FT PROPEP 345..353
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000030247"
FT TRANSMEM 29..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT TRANSMEM 118..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT TRANSMEM 142..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT TRANSMEM 197..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT TRANSMEM 274..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 118
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="ChlzD1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 126
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 170
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 189
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 198
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="PD1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 215
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
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_01379"
FT BINDING 264..265
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 272
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_01379"
FT BINDING 332
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 333
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 342
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 344
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT SITE 161
FT /note="Tyrosine radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT SITE 190
FT /note="Stabilizes free radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT SITE 344..345
FT /note="Cleavage; by CTPA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:3121625"
FT MOD_RES 2
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:3121625"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 32..54
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 87..91
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 110..136
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 196..220
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 268..293
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 332..336
FT /evidence="ECO:0007829|PDB:3JCU"
SQ SEQUENCE 353 AA; 38951 MW; BAD3F384DAB4D602 CRC64;
MTAILERRES ESLWGRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI
DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL
LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYRFG
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF
NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAAIEAPS TNG
