ID A0A1R3L2Z4_9ROSI Unreviewed; 353 AA.
AC A0A1R3L2Z4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Photosystem II D2 protein {ECO:0000256|HAMAP-Rule:MF_01383, ECO:0000256|RuleBase:RU004333};
DE Short=PSII D2 protein {ECO:0000256|HAMAP-Rule:MF_01383};
DE EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01383};
DE AltName: Full=Photosystem Q(A) protein {ECO:0000256|HAMAP-Rule:MF_01383};
GN Name=psbD {ECO:0000256|HAMAP-Rule:MF_01383,
GN ECO:0000313|EMBL:QDS78382.1};
GN ORFNames=COLO4_01093 {ECO:0000313|EMBL:OMP13716.1};
OS Corchorus olitorius.
OG Plastid; Chloroplast {ECO:0000313|EMBL:QDS78382.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=93759 {ECO:0000313|EMBL:OMP13716.1, ECO:0000313|Proteomes:UP000187203};
RN [1] {ECO:0000313|Proteomes:UP000187203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RT "Corchorus olitorius genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OMP13716.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole seedlings {ECO:0000313|EMBL:OMP13716.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:OMP13716.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole seedlings {ECO:0000313|EMBL:OMP13716.1};
RX PubMed=28134914;
RA Islam M.S., Saito J.A., Emdad E.M., Ahmed B., Islam M.M., Halim A.,
RA Hossen Q.M., Hossain M.Z., Ahmed R., Hossain M.S., Kabir S.M., Khan M.S.,
RA Khan M.M., Hasan R., Aktar N., Honi U., Islam R., Rashid M.M., Wan X.,
RA Hou S., Haque T., Azam M.S., Moosa M.M., Elias S.M., Hasan A.M.,
RA Mahmood N., Shafiuddin M., Shahid S., Shommu N.S., Jahan S., Roy S.,
RA Chowdhury A., Akhand A.I., Nisho G.M., Uddin K.S., Rabeya T., Hoque S.M.,
RA Snigdha A.R., Mortoza S., Matin S.A., Islam M.K., Lashkar M.Z., Zaman M.,
RA Yuryev A., Uddin M.K., Rahman M.S., Haque M.S., Alam M.M., Khan H.,
RA Alam M.;
RT "Comparative genomics of two jute species and insight into fibre
RT biogenesis.";
RL Nat. Plants 3:0-0(2017).
RN [4] {ECO:0000313|EMBL:QDS78382.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang L.;
RT "The complete chloroplast genome sequences of Corchorus capsularis and C.
RT olitorius: organization and phylogenetic relationships to other species of
RT the Malvaceae family.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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. D2 is needed for assembly of a stable
CC PSII complex. {ECO:0000256|HAMAP-Rule:MF_01383}.
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|ARBA:ARBA00001833, ECO:0000256|HAMAP-
CC Rule:MF_01383};
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_01383}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid,
CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01383};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01383}.
CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC are entirely coordinated by water. {ECO:0000256|HAMAP-Rule:MF_01383}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000256|ARBA:ARBA00008204, ECO:0000256|HAMAP-Rule:MF_01383,
CC ECO:0000256|RuleBase:RU004331}.
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DR EMBL; AWUE01003462; OMP13716.1; -; Genomic_DNA.
DR EMBL; MK251465; QDS78382.1; -; Genomic_DNA.
DR SMR; A0A1R3L2Z4; -.
DR STRING; 93759.A0A1R3L2Z4; -.
DR OrthoDB; 0at2759; -.
DR Proteomes; UP000187203; Unassembled WGS sequence.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR CDD; cd09288; Photosystem-II_D2; 1.
DR Gene3D; 1.20.85.10; Photosystem II protein D1-like; 1.
DR HAMAP; MF_01383; PSII_PsbD_D2; 1.
DR InterPro; IPR036854; Photo_II_D1/D2_sf.
DR InterPro; IPR000484; Photo_RC_L/M.
DR InterPro; IPR005868; PSII_PsbD/D2.
DR NCBIfam; TIGR01152; psbD; 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 Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP-
KW Rule:MF_01383}; Chloroplast {ECO:0000313|EMBL:QDS78382.1};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP-
KW Rule:MF_01383};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_01383};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01383};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01383};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01383};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01383}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01383};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_01383};
KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW Rule:MF_01383}; Plastid {ECO:0000313|EMBL:QDS78382.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187203};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01383};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01383};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01383};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01383}.
FT TRANSMEM 28..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..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..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..292
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="ChlzD2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT BINDING 130
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT BINDING 143
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT BINDING 198
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="PD2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
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_01383"
FT BINDING 215
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="Q(A)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT BINDING 262
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="Q(A)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01383"
FT BINDING 269
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_01383"
SQ SEQUENCE 353 AA; 39535 MW; 8F2BC6DE33BD129C CRC64;
MTIALGKFTK DENDLFDIMD DWLRRDRFVF VGWSGLLLFP CAYFAVGGWF TGTTFVTSWY
THGLASSYLE GCNFLTAAVS TPANSLAHSL LLLWGPEAQG DFTRWCQLGG LWTFVALHGA
FGLIGFMLRQ FELARSVQLR PYNAIAFSGP IAVFVSVFLI YPLGQSGWFF APSFGVAAIF
RFILFFQGFH NWTLNPFHMM GVAGVLGAAL LCAIHGATVE NTLFEDGDGA NTFRAFNPTQ
AEETYSMVTA NRFWSQIFGV AFSNKRWLHF FMLFVPVTGL WMSALGVVGL ALNLRAYDFV
SQEIRAAEDP EFETFYTKNI LLNEGIRAWM AAQDQPHENL IFPEEVLPRG NAL
//
