PSBA3_THEVB
ID PSBA3_THEVB Reviewed; 360 AA.
AC Q8DIV4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Photosystem II protein D1 3 {ECO:0000255|HAMAP-Rule:MF_01379};
DE Short=PSII D1 protein 3 {ECO:0000255|HAMAP-Rule:MF_01379};
DE EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379};
DE AltName: Full=Photosystem II Q(B) protein 3 {ECO:0000255|HAMAP-Rule:MF_01379};
DE Flags: Precursor;
GN Name=psbA3 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305};
GN OrderedLocusNames=tlr1477;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP TOPOLOGY.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=19219048; DOI=10.1038/nsmb.1559;
RA Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
RT "Cyanobacterial photosystem II at 2.9-A resolution and the role of
RT quinones, lipids, channels and chloride.";
RL Nat. Struct. Mol. Biol. 16:334-342(2009).
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 ECO:0000269|PubMed:19219048}.
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, ECO:0000269|PubMed:19219048};
CC -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC dimeric complexes (By similarity) (PubMed:19219048). Precursor protein
CC interacts with Ycf48 (By similarity). {ECO:0000250|UniProtKB:P0A444,
CC ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:19219048}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01379, ECO:0000269|PubMed:19219048}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:19219048}.
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 -!- 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 -!- MASS SPECTROMETRY: Mass=38144; Mass_error=224; Method=MALDI; Note=Mass
CC for C-terminally truncated D1. The measured protein is probably a
CC mixture of the product of the 3 psbA genes.;
CC Evidence={ECO:0000269|PubMed:19219048};
CC -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of the
CC psbA gene. {ECO:0000255|HAMAP-Rule:MF_01379,
CC ECO:0000269|PubMed:12240834}.
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; BA000039; BAC09029.1; -; Genomic_DNA.
DR RefSeq; NP_682267.1; NC_004113.1.
DR RefSeq; WP_011057317.1; NC_004113.1.
DR AlphaFoldDB; Q8DIV4; -.
DR SMR; Q8DIV4; -.
DR STRING; 197221.22295202; -.
DR EnsemblBacteria; BAC09029; BAC09029; BAC09029.
DR KEGG; tel:tlr1477; -.
DR PATRIC; fig|197221.4.peg.1549; -.
DR eggNOG; ENOG502Z87P; Bacteria.
DR OMA; VWERFCS; -.
DR OrthoDB; 382342at2; -.
DR Proteomes; UP000000440; Chromosome.
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:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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; Chromophore; Electron transport;
KW Herbicide resistance; Iron; Magnesium; Manganese; Membrane; Metal-binding;
KW Oxidoreductase; Photosynthesis; Photosystem II; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19219048"
FT CHAIN 2..344
FT /note="Photosystem II protein D1 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000316374"
FT PROPEP 345..360
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000316375"
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"
SQ SEQUENCE 360 AA; 39757 MW; 4939CB488233DDD8 CRC64;
MTTVLQRREQ LNLWEQFCSW VTSTNNRLYV GWFGVLMIPT LLAATICFVI AFIAAPPVDI
DGIREPVSGS LLYGNNIITG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLIIFHFL
IGVFCYMGRE WELSYRLGMR PWICVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF
NFMLVFQAEH NILMHPFHQL GVAGVFGGAL FSAMHGSLVT SSLIRETTET ESANYGYKFG
QEEETYNIVA AHGYFGRLIF QYASFNNSRA LHFFLAAWPV IGIWFTALGI STMAFNLNGF
NFNHSVVDAQ GNVINTWADI INRANLGMEV MHERNAHNFP LDLASAESAP VAMIAPSING
