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Protein

Photosystem II protein D1

Gene

psbA1

more
Organism
Prochlorococcus marinus (strain MIT 9515)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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)DescriptionActionsGraphical viewLength
Metal bindingi119Magnesium (chlorophyll-a ChlzD1 axial ligand); via tele nitrogenUniRule annotation1
Binding sitei127Pheophytin D1UniRule annotation1
Sitei162Tyrosine radical intermediateUniRule annotation1
Metal bindingi171Calcium-manganese-oxide [Ca-4Mn-5O]; calciumUniRule annotation1
Metal bindingi171Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation1
Metal bindingi190Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation1
Sitei191Stabilizes free radical intermediateUniRule annotation1
Metal bindingi199Magnesium (chlorophyll-a PD1 axial ligand); via tele nitrogenUniRule annotation1
Metal bindingi216Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation1
Binding sitei216Quinone (B)UniRule annotation1
Metal bindingi273Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation1
Metal bindingi333Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; via tele nitrogenUniRule annotation1
Metal bindingi334Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3UniRule annotation1
Metal bindingi334Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation1
Metal bindingi343Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation1
Metal bindingi343Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2UniRule annotation1
Metal bindingi345Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via carboxylateUniRule annotation1
Metal bindingi345Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2; via carboxylateUniRule annotation1

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

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:psbA1UniRule annotationCurated
Ordered Locus Names:P9515_02531
AND
Name:psbA2UniRule annotationCurated
Ordered Locus Names:P9515_02551
OrganismiProchlorococcus marinus (strain MIT 9515)
Taxonomic identifieri167542 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001589 Componenti: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei30 – 47HelicalUniRule annotationAdd BLAST18
Transmembranei119 – 134HelicalUniRule annotationAdd BLAST16
Transmembranei143 – 157HelicalUniRule annotationAdd BLAST15
Transmembranei198 – 219HelicalUniRule annotationAdd BLAST22
Transmembranei275 – 289HelicalUniRule annotationAdd BLAST15

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Photosystem II, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003163651 – 345Photosystem II protein D1UniRule annotationAdd BLAST345
PropeptideiPRO_0000316366346 – 360UniRule annotationAdd BLAST15

Post-translational modificationi

Tyr-162 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)DescriptionActionsGraphical viewLength
Sitei345 – 346Cleavage; by CtpAUniRule annotation2

Interactioni

Subunit structurei

Cyanobacterial 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 PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.UniRule annotation

Protein-protein interaction databases

STRINGi167542.P9515_02551.

Structurei

3D structure databases

ProteinModelPortaliA2BUK1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni265 – 266Quinone (B)UniRule annotation2

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105EY5. Bacteria.
ENOG410XPX5. LUCA.
HOGENOMiHOG000246913.
KOiK02703.
OMAiCFTIAFI.
OrthoDBiPOG091H15P4.

Family and domain databases

Gene3Di1.20.85.10. 1 hit.
HAMAPiMF_01379. PSII_PsbA_D1. 1 hit.
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.

A2BUK1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTIQQQRTS LLKGWPQFCE WVTSTNNRIY VGWFGVLMIP CLLAAAACFI
60 70 80 90 100
VAFIAAPPVD IDGIREPVAG SFLYGNNIIS GAVVPSSNAI GLHFYPIWEA
110 120 130 140 150
ATVDEWLYNG GPYQLVIFHF LIGISAYMGR QWELSYRLGM RPWICVAYSA
160 170 180 190 200
PVSAAFAVFL VYPFGQGSFS DGMPLGISGT FNFMFVFQAE HNILMHPFHM
210 220 230 240 250
AGVAGMFGGS LFSAMHGSLV TSSLIRETTE TESQNYGYKF GQEEETYNIV
260 270 280 290 300
AAHGYFGRLI FQYASFNNSR SLHFFLAVFP VVCVWLTSMG ICTMAFNLNG
310 320 330 340 350
FNFNQSVVDA NGKIVPTWGD VLNRANLGME VMHERNAHNF PLDLAAAEST
360
TVALTAPAIG
Length:360
Mass (Da):39,636
Last modified:February 20, 2007 - v1
Checksum:i1F753283412DF22A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000552 Genomic DNA. Translation: ABM71462.1.
CP000552 Genomic DNA. Translation: ABM71464.1.
RefSeqiWP_011131862.1. NC_008817.1.

Genome annotation databases

EnsemblBacteriaiABM71462; ABM71462; P9515_02531.
ABM71464; ABM71464; P9515_02551.
KEGGipmc:P9515_02531.
pmc:P9515_02551.
PATRICi23014026. VBIProMar113831_0256.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000552 Genomic DNA. Translation: ABM71462.1.
CP000552 Genomic DNA. Translation: ABM71464.1.
RefSeqiWP_011131862.1. NC_008817.1.

3D structure databases

ProteinModelPortaliA2BUK1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167542.P9515_02551.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM71462; ABM71462; P9515_02531.
ABM71464; ABM71464; P9515_02551.
KEGGipmc:P9515_02531.
pmc:P9515_02551.
PATRICi23014026. VBIProMar113831_0256.

Phylogenomic databases

eggNOGiENOG4105EY5. Bacteria.
ENOG410XPX5. LUCA.
HOGENOMiHOG000246913.
KOiK02703.
OMAiCFTIAFI.
OrthoDBiPOG091H15P4.

Family and domain databases

Gene3Di1.20.85.10. 1 hit.
HAMAPiMF_01379. PSII_PsbA_D1. 1 hit.
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...

Entry informationi

Entry nameiPSBA_PROM5
AccessioniPrimary (citable) accession number: A2BUK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 20, 2007
Last modified: November 30, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Cyanobacteria usually contain more than 2 copies of the psbA gene.UniRule annotation
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

Documents

  1. 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.