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Protein

Photosystem II protein D1

Gene

psbA1

more
Organism
Prochlorococcus marinus (strain AS9601)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi119 – 1191Magnesium (chlorophyll-a ChlzD1 axial ligand); via tele nitrogenUniRule annotation
Binding sitei127 – 1271Pheophytin D1UniRule annotation
Sitei162 – 1621Tyrosine radical intermediateUniRule annotation
Metal bindingi171 – 1711Calcium-manganese-oxide [Ca-4Mn-5O]; calciumUniRule annotation
Metal bindingi171 – 1711Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation
Metal bindingi190 – 1901Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation
Sitei191 – 1911Stabilizes free radical intermediateUniRule annotation
Metal bindingi199 – 1991Magnesium (chlorophyll-a PD1 axial ligand); via tele nitrogenUniRule annotation
Metal bindingi216 – 2161Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation
Binding sitei216 – 2161Quinone (B)UniRule annotation
Metal bindingi273 – 2731Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation
Metal bindingi333 – 3331Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; via tele nitrogenUniRule annotation
Metal bindingi334 – 3341Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3UniRule annotation
Metal bindingi334 – 3341Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation
Metal bindingi343 – 3431Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation
Metal bindingi343 – 3431Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2UniRule annotation
Sitei345 – 3462Cleavage; by CtpAUniRule annotation
Metal bindingi345 – 3451Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via carboxylateUniRule annotation
Metal bindingi345 – 3451Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2; via carboxylateUniRule annotation

GO - Molecular functioni

  1. chlorophyll binding Source: UniProtKB-HAMAP
  2. electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity Source: InterPro
  3. iron ion binding Source: UniProtKB-HAMAP
  4. oxygen evolving activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. photosynthetic electron transport in photosystem II Source: InterPro
  2. protein-chromophore linkage Source: UniProtKB-KW
  3. response to herbicide Source: UniProtKB-KW
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

BioCyciPMAR146891:GH90-1276-MONOMER.
PMAR146891:GH90-247-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:psbA1UniRule annotationCurated
Ordered Locus Names:A9601_02441
AND
Name:psbA2UniRule annotationCurated
Ordered Locus Names:A9601_12521
OrganismiProchlorococcus marinus (strain AS9601)
Taxonomic identifieri146891 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002590 Componenti: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei30 – 4718HelicalUniRule annotationAdd
BLAST
Transmembranei119 – 13416HelicalUniRule annotationAdd
BLAST
Transmembranei143 – 15715HelicalUniRule annotationAdd
BLAST
Transmembranei198 – 21922HelicalUniRule annotationAdd
BLAST
Transmembranei275 – 28915HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. photosystem II Source: UniProtKB-KW
  3. thylakoid membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Photosystem II, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Photosystem II protein D1UniRule annotationPRO_0000316355Add
BLAST
Propeptidei346 – 36015UniRule annotationPRO_0000316356Add
BLAST

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

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

STRINGi146891.A9601_12521.

Structurei

3D structure databases

ProteinModelPortaliA2BP21.
SMRiA2BP21. Positions 15-345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni265 – 2662Quinone (B)UniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG04871.
HOGENOMiHOG000246913.
KOiK02703.
OMAiCFTIAFI.
OrthoDBiEOG6Q2SGP.

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.

A2BP21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTIQQQRSS LLKGWPQFCE WVTSTNNRIY VGWFGVLMIP CLLTAAACFI
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
TVALSAPAIG
Length:360
Mass (Da):39,638
Last modified:February 20, 2007 - v1
Checksum:iE8389C98C87541E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000551 Genomic DNA. Translation: ABM69532.1.
CP000551 Genomic DNA. Translation: ABM70536.1.
RefSeqiYP_001008639.1. NC_008816.1.
YP_001009643.1. NC_008816.1.

Genome annotation databases

EnsemblBacteriaiABM69532; ABM69532; A9601_02441.
ABM70536; ABM70536; A9601_12521.
KEGGipmb:A9601_02441.
pmb:A9601_12521.
PATRICi22981935. VBIProMar75723_0244.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000551 Genomic DNA. Translation: ABM69532.1.
CP000551 Genomic DNA. Translation: ABM70536.1.
RefSeqiYP_001008639.1. NC_008816.1.
YP_001009643.1. NC_008816.1.

3D structure databases

ProteinModelPortaliA2BP21.
SMRiA2BP21. Positions 15-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi146891.A9601_12521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM69532; ABM69532; A9601_02441.
ABM70536; ABM70536; A9601_12521.
KEGGipmb:A9601_02441.
pmb:A9601_12521.
PATRICi22981935. VBIProMar75723_0244.

Phylogenomic databases

eggNOGiNOG04871.
HOGENOMiHOG000246913.
KOiK02703.
OMAiCFTIAFI.
OrthoDBiEOG6Q2SGP.

Enzyme and pathway databases

BioCyciPMAR146891:GH90-1276-MONOMER.
PMAR146891:GH90-247-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AS9601.

Entry informationi

Entry nameiPSBA_PROMS
AccessioniPrimary (citable) accession number: A2BP21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 20, 2007
Last modified: April 1, 2015
This is version 64 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

External Data

Dasty 3

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 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.