PSBA_CHLRE
ID PSBA_CHLRE Reviewed; 352 AA.
AC P07753; B7U1G3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 150.
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:16453578};
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 Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16453578; DOI=10.1002/j.1460-2075.1984.tb02206.x;
RA Erickson J.M., Rahire M., Rochaix J.-D.;
RT "Chlamydomonas reinhardii gene for the 32,000 mol. wt. protein of
RT photosystem II contains four large introns and is located entirely within
RT the chloroplast inverted repeat.";
RL EMBO J. 3:2753-2762(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [3]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
RN [4]
RP MUTAGENESIS FOR HERBICIDE RESISTANCE.
RA Johanningmeier U., Bodner U., Wildner G.F.;
RT "A new mutation in the gene coding for the herbicide-binding protein in
RT Chlamydomonas.";
RL FEBS Lett. 211:221-224(1987).
RN [5]
RP MUTAGENESIS FOR HERBICIDE RESISTANCE.
RX PubMed=2535507; DOI=10.2307/3869015;
RA Erickson J.M., Pfister K., Rahire M., Togasaki R.K., Mets L.,
RA Rochaix J.-D.;
RT "Molecular and biophysical analysis of herbicide-resistant mutants of
RT Chlamydomonas reinhardtii: structure-function relationship of the
RT photosystem II D1 polypeptide.";
RL Plant Cell 1:361-371(1989).
RN [6]
RP MUTAGENESIS FOR HERBICIDE RESISTANCE.
RA Wildner G.F., Heisterkamp U., Trebst A.;
RT "Herbicide cross-resistance and mutations of the psbA gene in Chlamydomonas
RT reinhardtii.";
RL Z. Naturforsch. C 45:1142-1150(1990).
RN [7]
RP MUTAGENESIS FOR HERBICIDE RESISTANCE.
RX PubMed=1840907; DOI=10.2307/3869286;
RA Przibilla E., Heiss S., Johanningmeier U., Trebst A.;
RT "Site-specific mutagenesis of the D1 subunit of photosystem II in wild-type
RT Chlamydomonas.";
RL Plant Cell 3:169-174(1991).
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 -!- 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; X01424; CAA25670.1; -; Genomic_DNA.
DR EMBL; X02347; CAA25670.1; JOINED; Genomic_DNA.
DR EMBL; X02348; CAA25670.1; JOINED; Genomic_DNA.
DR EMBL; X02349; CAA25670.1; JOINED; Genomic_DNA.
DR EMBL; X02350; CAA25670.1; JOINED; Genomic_DNA.
DR EMBL; FJ423446; ACJ50111.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50144.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00922.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00957.1; -; Genomic_DNA.
DR PIR; A22780; A22780.
DR RefSeq; NP_958377.1; NC_005353.1.
DR RefSeq; NP_958413.1; NC_005353.1.
DR PDB; 6KAC; EM; 2.70 A; A/a=1-352.
DR PDB; 6KAD; EM; 3.40 A; A/a=1-352.
DR PDB; 6KAF; EM; 3.73 A; A/a=1-352.
DR PDBsum; 6KAC; -.
DR PDBsum; 6KAD; -.
DR PDBsum; 6KAF; -.
DR AlphaFoldDB; P07753; -.
DR SMR; P07753; -.
DR STRING; 3055.DAA00922; -.
DR ChEMBL; CHEMBL2268003; -.
DR PaxDb; P07753; -.
DR PRIDE; P07753; -.
DR GeneID; 2716969; -.
DR GeneID; 2716987; -.
DR KEGG; cre:ChreCp021; -.
DR KEGG; cre:ChreCp057; -.
DR eggNOG; ENOG502QR09; Eukaryota.
DR HOGENOM; CLU_054206_1_0_1; -.
DR InParanoid; P07753; -.
DR OrthoDB; 801765at2759; -.
DR BioCyc; MetaCyc:CHRECP057-MON; -.
DR Proteomes; UP000006906; 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 Electron transport; Herbicide resistance; Iron; Magnesium; Manganese;
KW Membrane; Metal-binding; Oxidoreductase; Phosphoprotein; Photosynthesis;
KW Photosystem II; Plastid; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT CHAIN 2..344
FT /note="Photosystem II protein D1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000090432"
FT PROPEP 345..352
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000316443"
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 MOD_RES 2
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT MUTAGEN 219
FT /note="V->I: Herbicide resistance."
FT MUTAGEN 251
FT /note="A->V: Herbicide resistance."
FT MUTAGEN 256
FT /note="G->D: Herbicide resistance."
FT MUTAGEN 264
FT /note="S->A: Herbicide resistance."
FT MUTAGEN 266
FT /note="N->T: Herbicide resistance."
FT MUTAGEN 275
FT /note="L->F: Herbicide resistance."
FT MUTAGEN 275
FT /note="L->P: Herbicide resistance."
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 87..91
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 110..136
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 196..220
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 268..294
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 330..336
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:6KAC"
SQ SEQUENCE 352 AA; 39042 MW; 844E0252B42421AB CRC64;
MTAILERREN SSLWARFCEW ITSTENRLYI GWFGVIMIPC LLTATSVFII AFIAAPPVDI
DGIREPVSGS LLYGNNIITG AVIPTSNAIG LHFYPIWEAA SLDEWLYNGG PYQLIVCHFL
LGVYCYMGRE WELSFRLGMR PWIAVAYSAP VAAASAVFLV YPIGQGSFSD GMPLGISGTF
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYRFG
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV IGIWFTALGL STMAFNLNGF
NFNQSVVDSQ GRVLNTWADI INRANLGMEV MHERNAHNFP LDLASTNSSS NN
