ID   PSBA2_SYNY3             Reviewed;         360 AA.
AC   P16033;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Photosystem II protein D1 2 {ECO:0000255|HAMAP-Rule:MF_01379};
DE            Short=PSII D1 protein 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01379};
DE   Flags: Precursor;
GN   Name=psbA2 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305};
GN   Synonyms=psbA-2; OrderedLocusNames=slr1311;
GN   and
GN   Name=psbA3 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305};
GN   Synonyms=psbA-3; OrderedLocusNames=sll1867;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2499875; DOI=10.1093/nar/17.10.3991;
RA   Ravnikar P.D., Debus R., Sevrinck J., Saetaert P., McIntosh L.;
RT   "Nucleotide sequence of a second psbA gene from the unicellular
RT   cyanobacterium Synechocystis 6803.";
RL   Nucleic Acids Res. 17:3991-3991(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2123543; DOI=10.1093/nar/18.22.6715;
RA   Metz J., Nixon P., Diner B.;
RT   "Nucleotide sequence of the psbA3 gene from the cyanobacterium
RT   Synechocystis PCC 6803.";
RL   Nucleic Acids Res. 18:6715-6715(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [4]
RP   MUTAGENESIS OF PHE-255; SER-264 AND LEU-271.
RX   PubMed=1498597; DOI=10.1105/tpc.4.3.273;
RA   Ohad N., Hirschberg J.;
RT   "Mutations in the D1 subunit of photosystem II distinguish between quinone
RT   and herbicide binding sites.";
RL   Plant Cell 4:273-282(1992).
RN   [5]
RP   MUTAGENESIS OF 221-SER-SER-222; 227-THR-THR-228; TYR-237; LYS-238 AND
RP   ARG-257.
RX   PubMed=8068689; DOI=10.1021/bi00200a035;
RA   Kless H., Oren-Shamir M., Malkin S., McIntosh L., Edelman M.;
RT   "The D-E region of the D1 protein is involved in multiple quinone and
RT   herbicide interactions in photosystem II.";
RL   Biochemistry 33:10501-10507(1994).
RN   [6]
RP   PROBABLE CLEAVAGE.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8034700; DOI=10.1016/s0021-9258(17)32175-0;
RA   Shestakov S.V., Anbudurai P.R., Stanbekova G.E., Gadzhiev A., Lind L.K.,
RA   Pakrasi H.B.;
RT   "Molecular cloning and characterization of the ctpA gene encoding a
RT   carboxyl-terminal processing protease. Analysis of a spontaneous
RT   photosystem II-deficient mutant strain of the cyanobacterium Synechocystis
RT   sp. PCC 6803.";
RL   J. Biol. Chem. 269:19354-19359(1994).
RN   [7]
RP   SUBCELLULAR LOCATION, AND LACK OF PHOSPHORYLATION.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=9512353; DOI=10.1016/s0014-5793(98)00088-x;
RA   Pursiheimo S., Rintamaeki E., Baena-Gonzalez E., Aro E.-M.;
RT   "Thylakoid protein phosphorylation in evolutionally divergent species with
RT   oxygenic photosynthesis.";
RL   FEBS Lett. 423:178-182(1998).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=12069591; DOI=10.1021/bi026012+;
RA   Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K.,
RA   Pakrasi H.B.;
RT   "Proteomic analysis of a highly active photosystem II preparation from the
RT   cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel
RT   polypeptides.";
RL   Biochemistry 41:8004-8012(2002).
RN   [9] {ECO:0007744|PDB:7N8O, ECO:0007744|PDB:7RCV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (1.93 ANGSTROMS) OF 11-344, FUNCTION,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=34937700; DOI=10.1073/pnas.2116765118;
RA   Gisriel C.J., Wang J., Liu J., Flesher D.A., Reiss K.M., Huang H.L.,
RA   Yang K.R., Armstrong W.H., Gunner M.R., Batista V.S., Debus R.J.,
RA   Brudvig G.W.;
RT   "High-resolution cryo-electron microscopy structure of photosystem II from
RT   the mesophilic cyanobacterium, Synechocystis sp. PCC 6803.";
RL   Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
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/PsbD) 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:34937700}.
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:34937700, ECO:0000312|PDB:7N8O};
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, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ),
CC       PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:12069591,
CC       ECO:0000269|PubMed:34937700}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01379, ECO:0000269|PubMed:12069591,
CC       ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:9512353}; Multi-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_01379,
CC       ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:9512353}.
CC   -!- PTM: C-terminally processed by CtpA; processing is essential to allow
CC       assembly of the oxygen-evolving complex and photosynthetic growth.
CC       {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:34937700,
CC       ECO:0000305|PubMed:8034700}.
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   -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of the
CC       psbA gene. {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; X56000; CAA39472.1; -; Genomic_DNA.
DR   EMBL; X13547; CAA31899.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18230.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA16586.1; -; Genomic_DNA.
DR   PIR; S13112; F2YB16.
DR   PDB; 6WJ6; EM; 2.58 A; A=1-360.
DR   PDB; 7N8O; EM; 1.93 A; A/a=11-344.
DR   PDB; 7RCV; EM; 2.01 A; A/a=11-344.
DR   PDB; 8AM5; EM; 3.10 A; A=1-344.
DR   PDB; 8ASL; EM; 3.15 A; A=1-344.
DR   PDBsum; 6WJ6; -.
DR   PDBsum; 7N8O; -.
DR   PDBsum; 7RCV; -.
DR   PDBsum; 8AM5; -.
DR   PDBsum; 8ASL; -.
DR   AlphaFoldDB; P16033; -.
DR   EMDB; EMD-15522; -.
DR   EMDB; EMD-15618; -.
DR   EMDB; EMD-21690; -.
DR   EMDB; EMD-24239; -.
DR   EMDB; EMD-24407; -.
DR   SMR; P16033; -.
DR   IntAct; P16033; 5.
DR   STRING; 1148.gene:10497441; -.
DR   TCDB; 3.E.2.2.2; the photosynthetic reaction center (prc) family.
DR   PaxDb; 1148-1651658; -.
DR   EnsemblBacteria; BAA16586; BAA16586; BAA16586.
DR   EnsemblBacteria; BAA18230; BAA18230; BAA18230.
DR   KEGG; syn:sll1867; -.
DR   KEGG; syn:slr1311; -.
DR   eggNOG; ENOG502Z87P; Bacteria.
DR   InParanoid; P16033; -.
DR   PhylomeDB; P16033; -.
DR   BRENDA; 1.10.3.9; 6192.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB.
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; Photosystem II protein D1-like; 2.
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   NCBIfam; TIGR01151; psbA; 1.
DR   PANTHER; PTHR33149; PHOTOSYSTEM II PROTEIN D1; 1.
DR   PANTHER; PTHR33149:SF12; PHOTOSYSTEM II PROTEIN D1; 1.
DR   Pfam; PF00124; Photo_RC; 1.
DR   PRINTS; PR00256; REACTNCENTRE.
DR   SUPFAM; SSF81483; Bacterial photosystem II reaction centre, L and M subunits; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 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   CHAIN           1..344
FT                   /note="Photosystem II protein D1 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000090493"
FT   PROPEP          345..360
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000305|PubMed:8034700"
FT                   /id="PRO_0000316429"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TRANSMEM        32..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TOPO_DOM        54..110
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TRANSMEM        111..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TOPO_DOM        135..142
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TRANSMEM        143..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TOPO_DOM        162..191
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TRANSMEM        192..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TOPO_DOM        219..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TRANSMEM        271..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   TOPO_DOM        296..360
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
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                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
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                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
FT   BINDING         147
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D1"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
FT   BINDING         170
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
FT   BINDING         189
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
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                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
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                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
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                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
FT   BINDING         264
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
FT   BINDING         265
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000269|PubMed:34937700,
FT                   ECO:0000312|PDB:7N8O"
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                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
FT   BINDING         332
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
FT   BINDING         333
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         337
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
FT   BINDING         342
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:34937700, ECO:0000312|PDB:7N8O"
FT   BINDING         344
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000305|PubMed:34937700, ECO:0000312|PDB:7N8O"
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                   ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:8034700,
FT                   ECO:0000312|PDB:7N8O"
FT   MUTAGEN         221..222
FT                   /note="SS->LA: Strong herbicide resistance."
FT                   /evidence="ECO:0000269|PubMed:8068689"
FT   MUTAGEN         227..228
FT                   /note="TT->AA: Herbicide resistance."
FT                   /evidence="ECO:0000269|PubMed:8068689"
FT   MUTAGEN         237
FT                   /note="Y->F: Weak herbicide resistance."
FT                   /evidence="ECO:0000269|PubMed:8068689"
FT   MUTAGEN         238
FT                   /note="K->V: Weak herbicide resistance."
FT                   /evidence="ECO:0000269|PubMed:8068689"
FT   MUTAGEN         255
FT                   /note="F->W: Herbicide resistance."
FT                   /evidence="ECO:0000269|PubMed:1498597"
FT   MUTAGEN         257
FT                   /note="R->V: Herbicide resistance."
FT                   /evidence="ECO:0000269|PubMed:8068689"
FT   MUTAGEN         264
FT                   /note="S->A: Strong herbicide resistance."
FT                   /evidence="ECO:0000269|PubMed:1498597"
FT   MUTAGEN         271
FT                   /note="L->V,M,A,S: Herbicide resistance."
FT                   /evidence="ECO:0000269|PubMed:1498597"
FT   HELIX           13..21
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           31..54
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   TURN            87..91
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           102..107
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           110..136
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           143..158
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           160..165
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           168..170
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           176..190
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           192..194
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           196..221
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           233..236
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           248..258
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           261..263
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           268..293
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   TURN            294..296
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   STRAND          297..299
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   STRAND          309..311
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   HELIX           317..331
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   TURN            332..336
FT                   /evidence="ECO:0007829|PDB:7N8O"
FT   STRAND          339..341
FT                   /evidence="ECO:0007829|PDB:7N8O"
SQ   SEQUENCE   360 AA;  39721 MW;  2FE4088498A416C2 CRC64;
     MTTTLQQRES ASLWEQFCQW VTSTNNRIYV GWFGTLMIPT LLTATTCFII AFIAAPPVDI
     DGIREPVAGS LLYGNNIISG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLVVFHFL
     IGIFCYMGRQ WELSYRLGMR PWICVAYSAP VSAATAVFLI YPIGQGSFSD GMPLGISGTF
     NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLVRETTEV ESQNYGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLGAWPV IGIWFTAMGV STMAFNLNGF
     NFNQSILDSQ GRVIGTWADV LNRANIGFEV MHERNAHNFP LDLASGEQAP VALTAPAVNG
//