ID PSBA_MAIZE Reviewed; 353 AA.
AC P48183; Q546V9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 145.
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|Ref.1};
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 Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Surecropper;
RA Netto A.P., McIntyre D.J., Sathasivan K.S.;
RT "Maize psbA gene encoding the 32 kDa photosystem II protein.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [3]
RP PROTEIN SEQUENCE OF 2-8, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE,
RP PHOSPHORYLATION AT THR-2, AND ACETYLATION AT THR-2.
RC STRAIN=cv. Olenka; TISSUE=Bundle sheath cell, and Mesophyll cell;
RX PubMed=22833285; DOI=10.1002/pmic.201200196;
RA Fristedt R., Wasilewska W., Romanowska E., Vener A.V.;
RT "Differential phosphorylation of thylakoid proteins in mesophyll and bundle
RT sheath chloroplasts from maize plants grown under low or high light.";
RL Proteomics 12:2852-2861(2012).
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/PsbD) 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, Psb30/Ycf12, at least 3 peripheral proteins of the
CC oxygen-evolving complex and a large number of cofactors. It forms
CC dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01379}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:22833285}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}. Note=PSII is
CC more abundant in mesophyll than bundle sheath cells and more abundant
CC in grana than stroma lamellae in mesophyll cells.
CC {ECO:0000269|PubMed:22833285}.
CC -!- PTM: Phosphorylated in both bundle sheath and mesophyll cells,
CC phosphorylation increases when cells are grown under high rather than
CC low light regimes (70 vs 900 umol photons/m-2/s).
CC {ECO:0000269|PubMed:22833285}.
CC -!- PTM: PSII is subject to light-induced damage, in particular to D1.
CC Damaged protein is degraded by Deg1 and FtsH proteases and replaced. In
CC maize mesophyll cells D1 degradation is less extensive in grana
CC (stacked) vs stroma (unstacked) lamellae, in part due to exclusion of
CC FtsH from the grana. D1 degradation is faster in bundle sheath cells.
CC {ECO:0000269|PubMed:22833285}.
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 -!- 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; AF543684; AAN33184.1; -; Genomic_DNA.
DR EMBL; X86563; CAA60265.1; -; Genomic_DNA.
DR PIR; S58531; S58531.
DR RefSeq; NP_043004.1; NC_001666.2.
DR AlphaFoldDB; P48183; -.
DR SMR; P48183; -.
DR STRING; 4577.P48183; -.
DR iPTMnet; P48183; -.
DR PaxDb; 4577-GRMZM5G844143_P01; -.
DR EnsemblPlants; Zm00001eb435340_T001; Zm00001eb435340_P001; Zm00001eb435340.
DR EnsemblPlants; Zm00001eb435620_T001; Zm00001eb435620_P001; Zm00001eb435620.
DR EnsemblPlants; Zm00001eb436890_T001; Zm00001eb436890_P001; Zm00001eb436890.
DR EnsemblPlants; Zm00001eb437100_T001; Zm00001eb437100_P001; Zm00001eb437100.
DR EnsemblPlants; Zm00001eb437310_T001; Zm00001eb437310_P001; Zm00001eb437310.
DR EnsemblPlants; Zm00001eb437750_T001; Zm00001eb437750_P001; Zm00001eb437750.
DR EnsemblPlants; Zm00001eb438280_T001; Zm00001eb438280_P001; Zm00001eb438280.
DR EnsemblPlants; Zm00001eb438290_T001; Zm00001eb438290_P001; Zm00001eb438290.
DR EnsemblPlants; Zm00001eb439910_T001; Zm00001eb439910_P001; Zm00001eb439910.
DR EnsemblPlants; Zm00001eb441950_T001; Zm00001eb441950_P001; Zm00001eb441950.
DR EnsemblPlants; Zm00001eb442710_T001; Zm00001eb442710_P001; Zm00001eb442710.
DR EnsemblPlants; Zm00001eb442990_T001; Zm00001eb442990_P001; Zm00001eb442990.
DR GeneID; 845199; -.
DR Gramene; Zm00001eb435340_T001; Zm00001eb435340_P001; Zm00001eb435340.
DR Gramene; Zm00001eb435620_T001; Zm00001eb435620_P001; Zm00001eb435620.
DR Gramene; Zm00001eb436890_T001; Zm00001eb436890_P001; Zm00001eb436890.
DR Gramene; Zm00001eb437100_T001; Zm00001eb437100_P001; Zm00001eb437100.
DR Gramene; Zm00001eb437310_T001; Zm00001eb437310_P001; Zm00001eb437310.
DR Gramene; Zm00001eb437750_T001; Zm00001eb437750_P001; Zm00001eb437750.
DR Gramene; Zm00001eb438280_T001; Zm00001eb438280_P001; Zm00001eb438280.
DR Gramene; Zm00001eb438290_T001; Zm00001eb438290_P001; Zm00001eb438290.
DR Gramene; Zm00001eb439910_T001; Zm00001eb439910_P001; Zm00001eb439910.
DR Gramene; Zm00001eb441950_T001; Zm00001eb441950_P001; Zm00001eb441950.
DR Gramene; Zm00001eb442710_T001; Zm00001eb442710_P001; Zm00001eb442710.
DR Gramene; Zm00001eb442990_T001; Zm00001eb442990_P001; Zm00001eb442990.
DR KEGG; zma:845199; -.
DR MaizeGDB; 105976; -.
DR eggNOG; ENOG502QR09; Eukaryota.
DR InParanoid; P48183; -.
DR OMA; CQWVTDT; -.
DR OrthoDB; 345654at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR Proteomes; UP000007305; Unassembled WGS sequence.
DR ExpressionAtlas; P48183; baseline and differential.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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; Photosystem II protein D1-like; 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 NCBIfam; TIGR01151; psbA; 1.
DR PANTHER; PTHR33149; PHOTOSYSTEM II PROTEIN D1; 1.
DR PANTHER; PTHR33149:SF12; PHOTOSYSTEM II PROTEIN D1; 1.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; Bacterial photosystem II reaction centre, L and M subunits; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 1: Evidence at protein level;
KW 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:22833285"
FT CHAIN 2..344
FT /note="Photosystem II protein D1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000090449"
FT PROPEP 345..353
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000316490"
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:22833285"
FT MOD_RES 2
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000269|PubMed:22833285"
SQ SEQUENCE 353 AA; 39011 MW; AA6BFB415FCE1C79 CRC64;
MTAILERRES TSLWGRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI
DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL
LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYKFG
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF
NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAALEVPY LNG
//
