ID U9VUQ8_9CYAN Unreviewed; 365 AA.
AC U9VUQ8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379};
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=psbA {ECO:0000256|HAMAP-Rule:MF_01379};
GN ORFNames=N836_09680 {ECO:0000313|EMBL:ESA35782.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA35782.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA35782.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA35782.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
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|ARBA:ARBA00037683,
CC 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, peripheral proteins PsbO, CyanoQ (PsbQ),
CC PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000256|HAMAP-Rule:MF_01379}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000256|ARBA:ARBA00004636, ECO:0000256|HAMAP-Rule:MF_01379};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004636,
CC ECO:0000256|HAMAP-Rule:MF_01379}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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: Cyanobacteriota usually contain more than 2 copies of
CC the psbA gene. {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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01379}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESA35782.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWNH01000053; ESA35782.1; -; Genomic_DNA.
DR RefSeq; WP_023073286.1; NZ_AWNH01000053.1.
DR AlphaFoldDB; U9VUQ8; -.
DR STRING; 1385935.N836_09680; -.
DR PATRIC; fig|1385935.3.peg.3351; -.
DR eggNOG; ENOG502Z87P; Bacteria.
DR OrthoDB; 505356at2; -.
DR Proteomes; UP000017515; Unassembled WGS sequence.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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 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 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}; Electron transport {ECO:0000256|HAMAP-Rule:MF_01379};
KW Herbicide resistance {ECO:0000256|ARBA:ARBA00022646, ECO:0000256|HAMAP-
KW Rule:MF_01379}; Iron {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}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_01379}; Photosystem II {ECO:0000256|HAMAP-Rule:MF_01379};
KW Reference proteome {ECO:0000313|Proteomes:UP000017515};
KW Thylakoid {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}; Transport {ECO:0000256|HAMAP-Rule:MF_01379}.
FT CHAIN 1..349
FT /note="Photosystem II protein D1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT /id="PRO_5023544163"
FT PROPEP 350..365
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT /id="PRO_5007351561"
FT TRANSMEM 29..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..300
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 277
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 337
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 338
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 347
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 349
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 349..350
FT /note="Cleavage; by CtpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
SQ SEQUENCE 365 AA; 40057 MW; 3D79CA500C824F73 CRC64;
MTTTLQRRDQ VGPWQQFCNW ITSTENRLYV GWFGVLMIPT LLAATACFVL AFIAAPPVDI
DGIREPVAGS LLLGNNIISG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLVIFHFL
IGIFAYMGRE WELSYRLGMR PWICVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF
NFMLVFQAEH NILMHPFHMM GVAGVFGGAL ISSMHGSLVT SSLVRETTEI ESQNYGYKFG
QEEETYNIVA AHGYFGRLVG RTNEILLGVD ANSRSLHFFM AAWPVIGIWF TALGISTMAF
NLNGFNFNQS ILDSQGRVIS TWADVINRAN LGMEVMHERN AHNFPLDLAS DEATPVAIAV
SSLAS
//
