ID   PSBA_ANTSP              Reviewed;         360 AA.
AC   P24625;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   10-OCT-2018, entry version 106.
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=Photosystem II Q(B) protein {ECO:0000255|HAMAP-Rule:MF_01379};
DE   Flags: Precursor;
GN   Name=psbA {ECO:0000255|HAMAP-Rule:MF_01379};
OS   Antithamnion sp. (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae;
OC   Ceramiales; Ceramiaceae; Antithamnion.
OX   NCBI_TaxID=2767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LB 95.79;
RX   PubMed=1934114; DOI=10.1007/BF00312783;
RA   Winhauer T., Jaeger S., Valentin K.-U., Zetsche K.;
RT   "Structural similarities between psbA genes from red and brown
RT   algae.";
RL   Curr. Genet. 20:177-180(1991).
CC   -!- FUNCTION: Photosystem II (PSII) is a light-driven water:
CC       plastoquinone oxidoreductase that uses light energy to abstract
CC       electrons from H(2)O, generating O(2) and a proton gradient
CC       subsequently used for ATP formation. It consists of a core antenna
CC       complex that captures photons, and an electron transfer chain that
CC       converts photonic excitation into a charge separation. The D1/D2
CC       (PsbA/PsbA) reaction center heterodimer binds P680, the primary
CC       electron donor of PSII as well as several subsequent electron
CC       acceptors. {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2
CC       plastoquinol. {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.
CC       It shares a non-heme iron and each subunit binds pheophytin,
CC       quinone, additional chlorophylls, carotenoids and lipids. D1
CC       provides most of the ligands for the Mn4-Ca-O5 cluster of the
CC       oxygen-evolving complex (OEC). There is also a Cl(-1) ion
CC       associated with D1 and D2, which is required for oxygen evolution.
CC       The PSII complex binds additional chlorophylls, carotenoids and
CC       specific lipids. {ECO:0000255|HAMAP-Rule:MF_01379};
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins
CC       PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL,
CC       PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC       proteins of the oxygen-evolving complex and a large number of
CC       cofactors. It forms dimeric complexes. {ECO:0000255|HAMAP-
CC       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
CC       redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- PTM: C-terminally processed by CTPA; processing is essential to
CC       allow assembly of the oxygen-evolving complex and thus
CC       photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and
CC       ChlD2) are entirely coordinated by water. {ECO:0000255|HAMAP-
CC       Rule:MF_01379}.
CC   -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil
CC       bind in the Q(B) binding site and block subsequent electron
CC       transfer. {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; X55364; CAA39049.1; -; Genomic_DNA.
DR   PIR; S32577; S32577.
DR   ProteinModelPortal; P24625; -.
DR   SMR; P24625; -.
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:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Calcium; Chlorophyll; Chloroplast; Chromophore; Electron transport;
KW   Herbicide resistance; Iron; Magnesium; Manganese; Membrane;
KW   Metal-binding; Oxidoreductase; Photosynthesis; Photosystem II;
KW   Plastid; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    344       Photosystem II protein D1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01379}.
FT                                /FTId=PRO_0000090424.
FT   PROPEP      345    360       {ECO:0000255|HAMAP-Rule:MF_01379}.
FT                                /FTId=PRO_0000316505.
FT   TRANSMEM     29     46       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   TRANSMEM    118    133       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   TRANSMEM    142    156       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   TRANSMEM    197    218       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   TRANSMEM    274    288       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   REGION      264    265       Quinone (B). {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       118    118       Magnesium (chlorophyll-a ChlzD1 axial
FT                                ligand); via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01379}.
FT   METAL       170    170       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                calcium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       170    170       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 4. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       189    189       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       198    198       Magnesium (chlorophyll-a PD1 axial
FT                                ligand); via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01379}.
FT   METAL       215    215       Iron; shared with heterodimeric partner;
FT                                via tele nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       272    272       Iron; shared with heterodimeric partner;
FT                                via tele nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       332    332       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01379}.
FT   METAL       333    333       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 3. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       333    333       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 4. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       342    342       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       342    342       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   METAL       344    344       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                calcium; via carboxylate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01379}.
FT   METAL       344    344       Calcium-manganese-oxide [Ca-4Mn-5O];
FT                                manganese 2; via carboxylate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01379}.
FT   BINDING     126    126       Pheophytin D1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   BINDING     215    215       Quinone (B). {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
FT   SITE        161    161       Tyrosine radical intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01379}.
FT   SITE        190    190       Stabilizes free radical intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01379}.
FT   SITE        344    345       Cleavage; by CTPA. {ECO:0000255|HAMAP-
FT                                Rule:MF_01379}.
SQ   SEQUENCE   360 AA;  39681 MW;  288EDE4685061F5F CRC64;
     MTATLERRES ASLWARFCTW ITMNENRLYI GWFGVVMIPT LLTATSVFII ACFAAPPVDI
     DGIREPVAGS LLYGNNIISG AIIPSSAAIG IHFYPIWEAA SLDEWLYNGG PYQLIVLHFL
     LGVCCYIGRE WEFSYRLGMR PWISVAFTAP VVAASAVFLV YPIGQGSFSD GMPLGISGTF
     NFMLVFQAEH NILMHPLHQL GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANNGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLGLWPV VGIWFTSMSV STMAFNLNGF
     NFNQSVVDSQ GRVINTWADI LNRANLGMEV MHERNAHNFP LDLASNESLP LALVAPAING
//