ID G7JG21_MEDTR Unreviewed; 353 AA.
AC G7JG21;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379, ECO:0000256|RuleBase:RU004332};
DE Short=PSII D1 protein {ECO:0000256|HAMAP-Rule:MF_01379};
DE EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01379};
DE AltName: Full=Photosystem II Q(B) protein {ECO:0000256|HAMAP-Rule:MF_01379};
GN Name=5333175 {ECO:0000313|EnsemblPlants:AES88246};
GN Synonyms=psbA {ECO:0000256|HAMAP-Rule:MF_01379,
GN ECO:0000313|EMBL:AFR59993.1};
GN OrderedLocusNames=MTR_4g051290 {ECO:0000313|EMBL:AES88246.1};
GN ORFNames=MtrunA17_Chr4g0016331 {ECO:0000313|EMBL:RHN59688.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OG Plastid {ECO:0000313|EMBL:AFR59993.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES88246.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES88246.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES88246.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES88246,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:AES88246.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES88246,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EMBL:AFR59993.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Paraggio {ECO:0000313|Proteomes:UP000002051};
RX PubMed=24644300; DOI=10.1093/dnares/dsu007;
RA Gurdon C., Maliga P.;
RT "Two Distinct Plastid Genome Configurations and Unprecedented Intraspecies
RT Length Variation in the accD Coding Region in Medicago truncatula.";
RL DNA Res. 21:417-427(2014).
RN [4] {ECO:0000313|EnsemblPlants:AES88246}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES88246};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [5] {ECO:0000313|EMBL:RHN59688.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN59688.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
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:0000256|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:0000256|HAMAP-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, Psb30/Ycf12, at least 3 peripheral proteins of the
CC oxygen-evolving complex and a large number of cofactors. It forms
CC dimeric complexes. {ECO:0000256|HAMAP-Rule:MF_01379}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01379}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01379}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:0000256|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:0000256|HAMAP-Rule:MF_01379}.
CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC are entirely coordinated by water. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01379}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000256|ARBA:ARBA00008204, ECO:0000256|HAMAP-Rule:MF_01379,
CC ECO:0000256|RuleBase:RU004331}.
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DR EMBL; CM001220; AES88246.1; -; Genomic_DNA.
DR EMBL; JX512022; AFR59993.1; -; Genomic_DNA.
DR EMBL; JX512023; AFR60069.1; -; Genomic_DNA.
DR EMBL; JX512024; AFR60145.1; -; Genomic_DNA.
DR EMBL; PSQE01000004; RHN59688.1; -; Genomic_DNA.
DR RefSeq; XP_003606049.1; XM_003606001.2.
DR RefSeq; YP_001381746.1; NC_003119.6.
DR AlphaFoldDB; G7JG21; -.
DR STRING; 3880.G7JG21; -.
DR PaxDb; 3880-AES88246; -.
DR EnsemblPlants; AES88246; AES88246; MTR_4g051290.
DR GeneID; 5333175; -.
DR Gramene; AES88246; AES88246; MTR_4g051290.
DR KEGG; mtr:5333175; -.
DR eggNOG; ENOG502QR09; Eukaryota.
DR HOGENOM; CLU_054206_1_0_1; -.
DR OMA; CQWVTDT; -.
DR OrthoDB; 1199614at2759; -.
DR Proteomes; UP000002051; Chromosome 4.
DR Proteomes; UP000002051; Plastid.
DR Proteomes; UP000265566; Chromosome 4.
DR GO; GO:0009523; C:photosystem II; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule.
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; 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 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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|HAMAP-Rule:MF_01379};
KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Herbicide resistance {ECO:0000256|ARBA:ARBA00022646, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01379};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01379};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01379};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01379};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379,
KW ECO:0000313|EMBL:RHN59688.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW Rule:MF_01379}; Plastid {ECO:0000313|EMBL:AFR59993.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01379};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01379}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT CHAIN 2..344
FT /note="Photosystem II protein D1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT /id="PRO_5035010023"
FT PROPEP 345..353
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT /id="PRO_5035010024"
FT TRANSMEM 29..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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:0000256|HAMAP-Rule:MF_01379"
FT BINDING 126
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 170
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 189
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01379"
FT BINDING 215
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="B"
FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01379"
FT BINDING 332
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 333
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 342
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 344
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT SITE 161
FT /note="Tyrosine radical intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT SITE 190
FT /note="Stabilizes free radical intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT SITE 344..345
FT /note="Cleavage; by CtpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT MOD_RES 2
FT /note="Phosphothreonine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
SQ SEQUENCE 353 AA; 38992 MW; E88613389BDBE4D5 CRC64;
MTAILERRDS ENLWSRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI
DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL
LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYRFG
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF
NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAAVEAPS ING
//