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Photosystem II protein D1 (PSII D1 protein) (EC 1.10.3.9) (Photosystem II Q(B) protein)

 Q9BBY5_PRUYE            Unreviewed;       353 AA.
Q9BBY5;
01-JUN-2001, integrated into UniProtKB/TrEMBL.
01-JUN-2001, sequence version 1.
27-SEP-2017, entry version 83.
RecName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004332};
Short=PSII D1 protein {ECO:0000256|HAMAP-Rule:MF_01379};
EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01379};
AltName: Full=Photosystem II Q(B) protein {ECO:0000256|HAMAP-Rule:MF_01379};
Name=psbA {ECO:0000256|HAMAP-Rule:MF_01379,
ECO:0000313|EMBL:AAG60671.1};
Prunus yedoensis (Yoshino cherry) (Cerasus yedoensis).
Plastid; Chloroplast {ECO:0000313|EMBL:AAG60671.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae;
Amygdaleae; Prunus.
NCBI_TaxID=3759 {ECO:0000313|EMBL:AAG60671.1};
[1] {ECO:0000313|EMBL:AAG60671.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Cheju native species {ECO:0000313|EMBL:AAG60671.1};
Jung Y.H., Han S.H., Ko M.H., Oh Y.S., Oh M.Y.;
"Prunus yedoensis-Cheju native species PSII D1 protein (psbA) gene.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Photosystem II (PSII) is a light-driven water:
plastoquinone oxidoreductase that uses light energy to abstract
electrons from H(2)O, generating O(2) and a proton gradient
subsequently used for ATP formation. It consists of a core antenna
complex that captures photons, and an electron transfer chain that
converts photonic excitation into a charge separation. The D1/D2
(PsbA/PsbA) reaction center heterodimer binds P680, the primary
electron donor of PSII as well as several subsequent electron
acceptors. {ECO:0000256|HAMAP-Rule:MF_01379}.
-!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2
plastoquinol. {ECO:0000256|HAMAP-Rule:MF_01379}.
-!- COFACTOR:
Note=The D1/D2 heterodimer binds P680, chlorophylls that are the
primary electron donor of PSII, and subsequent electron acceptors.
It shares a non-heme iron and each subunit binds pheophytin,
quinone, additional chlorophylls, carotenoids and lipids. D1
provides most of the ligands for the Mn4-Ca-O5 cluster of the
oxygen-evolving complex (OEC). There is also a Cl(-1) ion
associated with D1 and D2, which is required for oxygen evolution.
The PSII complex binds additional chlorophylls, carotenoids and
specific lipids. {ECO:0000256|HAMAP-Rule:MF_01379};
-!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins
PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL,
PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
proteins of the oxygen-evolving complex and a large number of
cofactors. It forms dimeric complexes. {ECO:0000256|HAMAP-
Rule:MF_01379}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000256|HAMAP-Rule:MF_01379}; Multi-pass membrane protein
{ECO:0000256|HAMAP-Rule:MF_01379}.
-!- PTM: C-terminally processed by CtpA; processing is essential to
allow assembly of the oxygen-evolving complex and thus
photosynthetic growth. {ECO:0000256|HAMAP-Rule:MF_01379}.
-!- PTM: Tyr-161 forms a radical intermediate that is referred to as
redox-active TyrZ, YZ or Y-Z. {ECO:0000256|HAMAP-Rule:MF_01379}.
-!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and
ChlD2) are entirely coordinated by water. {ECO:0000256|HAMAP-
Rule:MF_01379}.
-!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil
bind in the Q(B) binding site and block subsequent electron
transfer. {ECO:0000256|HAMAP-Rule:MF_01379}.
-!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
{ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004331}.
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EMBL; AF314010; AAG60671.1; -; Genomic_DNA.
ProteinModelPortal; Q9BBY5; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
CDD; cd09289; Photosystem-II_D1; 1.
Gene3D; 1.20.85.10; -; 2.
HAMAP; MF_01379; PSII_PsbA_D1; 1.
InterPro; IPR000484; Photo_RC_L/M.
InterPro; IPR005867; PSII_D1.
Pfam; PF00124; Photo_RC; 1.
PRINTS; PR00256; REACTNCENTRE.
SUPFAM; SSF81483; SSF81483; 1.
TIGRFAMs; TIGR01151; psbA; 1.
PROSITE; PS00244; REACTION_CENTER; 1.
3: Inferred from homology;
Calcium {ECO:0000256|HAMAP-Rule:MF_01379};
Chlorophyll {ECO:0000256|HAMAP-Rule:MF_01379};
Chloroplast {ECO:0000313|EMBL:AAG60671.1};
Chromophore {ECO:0000256|HAMAP-Rule:MF_01379};
Electron transport {ECO:0000256|HAMAP-Rule:MF_01379,
ECO:0000256|RuleBase:RU004332};
Herbicide resistance {ECO:0000256|HAMAP-Rule:MF_01379};
Iron {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004332};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01379};
Manganese {ECO:0000256|HAMAP-Rule:MF_01379};
Membrane {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01379,
ECO:0000256|RuleBase:RU004332};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379};
Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01379,
ECO:0000256|RuleBase:RU004332};
Photosystem II {ECO:0000256|HAMAP-Rule:MF_01379,
ECO:0000256|RuleBase:RU004332}; Plastid {ECO:0000313|EMBL:AAG60671.1};
Thylakoid {ECO:0000256|HAMAP-Rule:MF_01379};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01379,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01379,
ECO:0000256|SAM:Phobius};
Transport {ECO:0000256|HAMAP-Rule:MF_01379,
ECO:0000256|RuleBase:RU004332}.
INIT_MET 1 1 Removed. {ECO:0000256|HAMAP-
Rule:MF_01379}.
PROPEP 345 353 {ECO:0000256|HAMAP-Rule:MF_01379}.
/FTId=PRO_5007350258.
TRANSMEM 29 56 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 109 129 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 141 161 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 198 218 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 273 295 Helical. {ECO:0000256|SAM:Phobius}.
REGION 264 265 Quinone (B). {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 118 118 Magnesium (chlorophyll-a ChlzD1 axial
ligand); via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01379}.
METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O];
calcium. {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 4. {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 189 189 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 1. {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 198 198 Magnesium (chlorophyll-a PD1 axial
ligand); via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01379}.
METAL 215 215 Iron; shared with heterodimeric partner;
via tele nitrogen. {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 272 272 Iron; shared with heterodimeric partner;
via tele nitrogen. {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 332 332 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 1; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01379}.
METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 3. {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 4. {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 1. {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 2. {ECO:0000256|HAMAP-
Rule:MF_01379}.
METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O];
calcium; via carboxylate.
{ECO:0000256|HAMAP-Rule:MF_01379}.
METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 2; via carboxylate.
{ECO:0000256|HAMAP-Rule:MF_01379}.
BINDING 126 126 Pheophytin D1. {ECO:0000256|HAMAP-
Rule:MF_01379}.
BINDING 215 215 Quinone (B). {ECO:0000256|HAMAP-
Rule:MF_01379}.
SITE 161 161 Tyrosine radical intermediate.
{ECO:0000256|HAMAP-Rule:MF_01379}.
SITE 190 190 Stabilizes free radical intermediate.
{ECO:0000256|HAMAP-Rule:MF_01379}.
SITE 344 345 Cleavage; by CtpA. {ECO:0000256|HAMAP-
Rule:MF_01379}.
MOD_RES 2 2 N-acetylthreonine. {ECO:0000256|HAMAP-
Rule:MF_01379}.
MOD_RES 2 2 Phosphothreonine. {ECO:0000256|HAMAP-
Rule:MF_01379}.
SEQUENCE 353 AA; 38863 MW; F497CC8AD088D37E CRC64;
MTAILERRES ESLWGRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFIM ALIAAPPVDI
DGIREPVSGS LLYGNNIISR AIIPTSAAIG SHFYPIWEAA SVDEWLYDGG PYELIVLHFL
LGVACYMGRE LELSFRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLTREPTEN ETANDGSRFG
QEEETYNIVA AHGYFGRLFF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF
NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAAVEAPS TNG


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