Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Photosystem II protein D1

Gene

psbA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Photosystem II (PSII) is a light-driven water: plastoquinone oxidoreductase that uses light energy to abstract electrons from H2O, generating O2 and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.UniRule annotation

Catalytic activityi

2 H2O + 2 plastoquinone + 4 light = O2 + 2 plastoquinol.UniRule annotation

Cofactori

Note: The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi118 – 1181Magnesium (chlorophyll-a ChlzD1 axial ligand); via tele nitrogenUniRule annotation
Binding sitei126 – 1261Pheophytin D1UniRule annotation
Sitei161 – 1611Tyrosine radical intermediateUniRule annotation
Metal bindingi170 – 1701Calcium-manganese-oxide [Ca-4Mn-5O]; calciumUniRule annotation
Metal bindingi170 – 1701Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation
Metal bindingi189 – 1891Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation
Sitei190 – 1901Stabilizes free radical intermediateUniRule annotation
Metal bindingi198 – 1981Magnesium (chlorophyll-a PD1 axial ligand); via tele nitrogenUniRule annotation
Metal bindingi215 – 2151Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation
Binding sitei215 – 2151Quinone (B)UniRule annotation
Metal bindingi272 – 2721Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation
Metal bindingi332 – 3321Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; via tele nitrogenUniRule annotation
Metal bindingi333 – 3331Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3UniRule annotation
Metal bindingi333 – 3331Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation
Metal bindingi342 – 3421Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation
Metal bindingi342 – 3421Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2UniRule annotation
Metal bindingi344 – 3441Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via carboxylateUniRule annotation
Metal bindingi344 – 3441Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2; via carboxylateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Herbicide resistance, Photosynthesis, Transport

Keywords - Ligandi

Calcium, Chlorophyll, Chromophore, Iron, Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ATCG00020-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem II protein D1UniRule annotation (EC:1.10.3.9UniRule annotation)
Short name:
PSII D1 proteinUniRule annotation
Alternative name(s):
Photosystem II Q(B) proteinUniRule annotation
Gene namesi
Name:psbAUniRule annotation
Ordered Locus Names:AtCg00020
Encoded oniPlastid; Chloroplast
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chloroplast

Organism-specific databases

TAIRiATCG00020.

Subcellular locationi

  • Plastidchloroplast thylakoid membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei29 – 4618HelicalUniRule annotationAdd
BLAST
Transmembranei118 – 13316HelicalUniRule annotationAdd
BLAST
Transmembranei142 – 15615HelicalUniRule annotationAdd
BLAST
Transmembranei197 – 21822HelicalUniRule annotationAdd
BLAST
Transmembranei274 – 28815HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Photosystem II, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 344343Photosystem II protein D1UniRule annotationPRO_0000090425Add
BLAST
Propeptidei345 – 3539UniRule annotationPRO_0000316439

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineUniRule annotation1 Publication
Modified residuei2 – 21PhosphothreonineUniRule annotation1 Publication

Post-translational modificationi

Phosphorylation occurs in normal plant growth light conditions. Rapid dephosphorylation occurs during heat shock.1 Publication
Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.UniRule annotation
C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei344 – 3452Cleavage; by CTPAUniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP83755.
PRIDEiP83755.

PTM databases

iPTMnetiP83755.

Expressioni

Gene expression databases

GenevisibleiP83755. AT.

Interactioni

Subunit structurei

PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes (By similarity). Interacts with PAM68 (PubMed:20923938). The nascent chain still attached to the ribosome interacts with FFC/ cpSRP54, but not with CAO/cpSRP43 or SecA (PubMed:9927433).UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAM4P258542EBI-1236013,EBI-1235664
CAM7P592202EBI-1236013,EBI-1236031
CML9Q9S7442EBI-1236013,EBI-1236048

Protein-protein interaction databases

BioGridi29991. 9 interactions.
IntActiP83755. 10 interactions.
MINTiMINT-8360520.
STRINGi3702.ATCG00020.1.

Structurei

3D structure databases

ProteinModelPortaliP83755.
SMRiP83755. Positions 12-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni264 – 2652Quinone (B)UniRule annotation

Sequence similaritiesi

Belongs to the reaction center PufL/M/PsbA/D family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHF0. Eukaryota.
ENOG410XPX5. LUCA.
HOGENOMiHOG000246913.
InParanoidiP83755.
KOiK02703.
OMAiCFTIAFI.

Family and domain databases

Gene3Di1.20.85.10. 1 hit.
HAMAPiMF_01379. PSII_PsbA_D1.
InterProiIPR000484. Photo_RC_L/M.
IPR005867. PSII_D1.
[Graphical view]
PfamiPF00124. Photo_RC. 1 hit.
[Graphical view]
PRINTSiPR00256. REACTNCENTRE.
SUPFAMiSSF81483. SSF81483. 1 hit.
TIGRFAMsiTIGR01151. psbA. 1 hit.
PROSITEiPS00244. REACTION_CENTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P83755-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAILERRES ESLWGRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFII
60 70 80 90 100
AFIAAPPVDI DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA
110 120 130 140 150
SVDEWLYNGG PYELIVLHFL LGVACYMGRE WELSFRLGMR PWIAVAYSAP
160 170 180 190 200
VAAATAVFLI YPIGQGSFSD GMPLGISGTF NFMIVFQAEH NILMHPFHML
210 220 230 240 250
GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYRFG QEEETYNIVA
260 270 280 290 300
AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF
310 320 330 340 350
NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAAVEAPS

TNG
Length:353
Mass (Da):38,937
Last modified:January 23, 2007 - v2
Checksum:i79D3F384DAB4D610
GO

Mass spectrometryi

Molecular mass is 823.4 Da from positions 2 - 7. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79898 Genomic DNA. Translation: CAA56270.1.
AP000423 Genomic DNA. Translation: BAA84365.1.
PIRiS57265.
RefSeqiNP_051039.1. NC_000932.1.

Genome annotation databases

EnsemblPlantsiATCG00020.1; ATCG00020.1; ATCG00020.
GeneIDi844802.
GrameneiATCG00020.1; ATCG00020.1; ATCG00020.
KEGGiath:ArthCp002.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79898 Genomic DNA. Translation: CAA56270.1.
AP000423 Genomic DNA. Translation: BAA84365.1.
PIRiS57265.
RefSeqiNP_051039.1. NC_000932.1.

3D structure databases

ProteinModelPortaliP83755.
SMRiP83755. Positions 12-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi29991. 9 interactions.
IntActiP83755. 10 interactions.
MINTiMINT-8360520.
STRINGi3702.ATCG00020.1.

PTM databases

iPTMnetiP83755.

Proteomic databases

PaxDbiP83755.
PRIDEiP83755.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiATCG00020.1; ATCG00020.1; ATCG00020.
GeneIDi844802.
GrameneiATCG00020.1; ATCG00020.1; ATCG00020.
KEGGiath:ArthCp002.

Organism-specific databases

TAIRiATCG00020.

Phylogenomic databases

eggNOGiENOG410IHF0. Eukaryota.
ENOG410XPX5. LUCA.
HOGENOMiHOG000246913.
InParanoidiP83755.
KOiK02703.
OMAiCFTIAFI.

Enzyme and pathway databases

BioCyciMetaCyc:ATCG00020-MONOMER.

Miscellaneous databases

PROiP83755.

Gene expression databases

GenevisibleiP83755. AT.

Family and domain databases

Gene3Di1.20.85.10. 1 hit.
HAMAPiMF_01379. PSII_PsbA_D1.
InterProiIPR000484. Photo_RC_L/M.
IPR005867. PSII_D1.
[Graphical view]
PfamiPF00124. Photo_RC. 1 hit.
[Graphical view]
PRINTSiPR00256. REACTNCENTRE.
SUPFAMiSSF81483. SSF81483. 1 hit.
TIGRFAMsiTIGR01151. psbA. 1 hit.
PROSITEiPS00244. REACTION_CENTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of the Arabidopsis thaliana chloroplast DNA region containing the genes psbA, trnH and rps19'."
    Liere K., Kestermann M., Mueller U., Link G.
    Curr. Genet. 28:128-130(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  2. "Complete structure of the chloroplast genome of Arabidopsis thaliana."
    Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.
    DNA Res. 6:283-290(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana."
    Vener A.V., Harms A., Sussman M.R., Vierstra R.D.
    J. Biol. Chem. 276:6959-6966(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-7, PHOSPHORYLATION AT THR-2, ACETYLATION AT THR-2, MASS SPECTROMETRY.
    Strain: cv. Columbia.
  4. "Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54."
    Nilsson R., Brunner J., Hoffman N.E., van Wijk K.J.
    EMBO J. 18:733-742(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FFC/CPSRP54.
  5. "The Arabidopsis thylakoid protein PAM68 is required for efficient D1 biogenesis and photosystem II assembly."
    Armbruster U., Zuhlke J., Rengstl B., Kreller R., Makarenko E., Ruhle T., Schunemann D., Jahns P., Weisshaar B., Nickelsen J., Leister D.
    Plant Cell 22:3439-3460(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAM68.

Entry informationi

Entry nameiPSBA_ARATH
AccessioniPrimary (citable) accession number: P83755
Secondary accession number(s): Q33592
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water.UniRule annotation
Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer.UniRule annotation

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.