PSBA_EUGGR
ID PSBA_EUGGR Reviewed; 345 AA.
AC P06631;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 126.
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:6431398};
DE AltName: Full=Photosystem II Q(B) protein {ECO:0000255|HAMAP-Rule:MF_01379};
GN Name=psbA {ECO:0000255|HAMAP-Rule:MF_01379};
OS Euglena gracilis.
OG Plastid; Chloroplast.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Keller M., Stutz E.;
RT "Structure of the Euglena gracilis chloroplast gene (psbA) coding for the
RT 32-kDa protein of Photosystem II.";
RL FEBS Lett. 175:173-177(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6431398; DOI=10.1093/nar/12.14.5801;
RA Karabin G.D., Farley M.A., Hallick R.B.;
RT "Chloroplast gene for Mr 32000 polypeptide of photosystem II in Euglena
RT gracilis is interrupted by four introns with conserved boundary
RT sequences.";
RL Nucleic Acids Res. 12:5801-5812(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=8346031; DOI=10.1093/nar/21.15.3537;
RA Hallick R.B., Hong L., Drager R.G., Favreau M.R., Monfort A., Orsat B.,
RA Spielmann A., Stutz E.;
RT "Complete sequence of Euglena gracilis chloroplast DNA.";
RL Nucleic Acids Res. 21:3537-3544(1993).
RN [4]
RP MUTANT ALA-265.
RX PubMed=3129202; DOI=10.1007/bf00434825;
RA Johanningmeier U., Hallick R.B.;
RT "The psbA gene of DCMU-resistant Euglena gracilis has an amino acid
RT substitution at serine codon 265.";
RL Curr. Genet. 12:465-470(1987).
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-162 forms a radical intermediate that is referred to as redox-
CC active TyrZ, YZ or Y-Z. {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; Z11874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X00929; CAA25447.1; -; Genomic_DNA.
DR EMBL; X00735; CAA25319.1; -; Genomic_DNA.
DR EMBL; X70810; CAA50082.1; -; Genomic_DNA.
DR PIR; A22883; S34503.
DR RefSeq; NP_041895.1; NC_001603.2.
DR AlphaFoldDB; P06631; -.
DR SMR; P06631; -.
DR GeneID; 807514; -.
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: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 Calcium; Chlorophyll; Chloroplast; Chromophore; Electron transport;
KW Herbicide resistance; Iron; Magnesium; Manganese; Membrane; Metal-binding;
KW Oxidoreductase; Photosynthesis; Photosystem II; Plastid; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..345
FT /note="Photosystem II protein D1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000090440"
FT TRANSMEM 30..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT TRANSMEM 119..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT TRANSMEM 143..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT TRANSMEM 198..219
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT TRANSMEM 275..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 119
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 127
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 171
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 190
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 199
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 216
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 216
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 265..266
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 273
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 333
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 334
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 343
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT BINDING 345
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT SITE 162
FT /note="Tyrosine radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT SITE 191
FT /note="Stabilizes free radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT MUTAGEN 265
FT /note="S->A: Herbicide resistance."
FT CONFLICT 79
FT /note="I -> L (in Ref. 1; CAA25447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 38365 MW; C2F3B5435EAFFDAD CRC64;
MISPVLKKYA RPSLWYRFCA WVASKKNRLY VGWFGVLMIP TLLTAATVFI IAFIAAPPVD
IDGIREPVSG SLFYGNNIIT GAVVPTSNAI GLHFYPIWEA TSLDEWLYNG GPYQLIVCHF
FIGICSYMGR EWELSFRLGM RPWIAVAYSA PVAAASAVFI VYPLGQGSFS DGMPLGISGT
FNFMIVFQAE HNILMHPFHM LGVAGVFGGS LFSAMHGSLV TSSLLRETTE NESINVGYKF
GQEEETYNII AAHAYFGRLI FQYASFNNSR SLHFFLAVWP VVGIWFTALG VSTMAFNLNG
FNFNQSVIDS QGRVINTWAD IINRANLGME VMHERNAHNF PLDLA
