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Protein

Photosystem II protein D1

Gene

psbA1

more
Organism
Microcystis aeruginosa (strain NIES-843)
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 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
Sitei344 – 3452Cleavage; by CtpAUniRule 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

BioCyciMAER449447:GHO8-1024-MONOMER.
MAER449447:GHO8-1040-MONOMER.
MAER449447:GHO8-1053-MONOMER.
MAER449447:GHO8-1082-MONOMER.
MAER449447:GHO8-5862-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:MAE_10220
AND
Name:psbA2UniRule annotationCurated
Ordered Locus Names:MAE_10380
AND
Name:psbA3UniRule annotationCurated
Ordered Locus Names:MAE_10510
AND
Name:psbA4UniRule annotationCurated
Ordered Locus Names:MAE_10800
AND
Name:psbA5UniRule annotationCurated
Ordered Locus Names:MAE_58140
OrganismiMicrocystis aeruginosa (strain NIES-843)
Taxonomic identifieri449447 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesMicrocystis
ProteomesiUP000001510 Componenti: Chromosome

Subcellular locationi

  • Cellular 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

Membrane, Photosystem II, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Photosystem II protein D1UniRule annotationPRO_0000339926Add
BLAST
Propeptidei345 – 36016UniRule annotationPRO_0000339927Add
BLAST

Post-translational modificationi

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

Proteomic databases

PaxDbiB0JIS8.
PRIDEiB0JIS8.

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

STRINGi449447.MAE_58140.

Structurei

3D structure databases

ProteinModelPortaliB0JIS8.
SMRiB0JIS8. Positions 10-344.
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

eggNOGiNOG04871.
HOGENOMiHOG000246913.
KOiK02703.
OMAiTWITSTE.
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.

B0JIS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTTLQQRES ASLWEQFCQW ITSTNNRLYI GWFGVIMIPT LLTATTCFII
60 70 80 90 100
AFIAAPPVDI DGIREPVAGS LLYGNNIISG AVVPSSNAIG LHFYPIWEAA
110 120 130 140 150
SLDEWLYNGG PYQLVIFHFL LGVFCYLGRQ WELSFRLGMR PWICVAYSAP
160 170 180 190 200
VSAATAVFLI YPIGQGSFSD GMPLGISGTF NFMFVFQAEH NILMHPFHML
210 220 230 240 250
GVAGVFGGSL FSAMHGSLVT SSLVRETTEI ESQNYGYKFG QEEETYNIVA
260 270 280 290 300
AHGYFGRLIF QYASFNNSRS LHFFLGAWPV IGIWFTAMGV STMAFNLNGF
310 320 330 340 350
NFNQSILDSQ GRVIGTWADV LNRAGIGMEV MHERNAHNFP LDLASGEQAP
360
VALIAPAING
Length:360
Mass (Da):39,715
Last modified:March 18, 2008 - v1
Checksum:i68BDBFFC518BA80B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009552 Genomic DNA. Translation: BAG00844.1.
AP009552 Genomic DNA. Translation: BAG00860.1.
AP009552 Genomic DNA. Translation: BAG00873.1.
AP009552 Genomic DNA. Translation: BAG00902.1.
AP009552 Genomic DNA. Translation: BAG05636.1.
RefSeqiWP_012264511.1. NC_010296.1.
YP_001656036.1. NC_010296.1.
YP_001656052.1. NC_010296.1.
YP_001656065.1. NC_010296.1.
YP_001656094.1. NC_010296.1.
YP_001660828.1. NC_010296.1.

Genome annotation databases

EnsemblBacteriaiBAG00844; BAG00844; MAE_10220.
BAG00860; BAG00860; MAE_10380.
BAG00873; BAG00873; MAE_10510.
BAG00902; BAG00902; MAE_10800.
BAG05636; BAG05636; MAE_58140.
GeneIDi5866658.
KEGGimar:MAE_10220.
mar:MAE_10380.
mar:MAE_10510.
mar:MAE_10800.
mar:MAE_58140.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009552 Genomic DNA. Translation: BAG00844.1.
AP009552 Genomic DNA. Translation: BAG00860.1.
AP009552 Genomic DNA. Translation: BAG00873.1.
AP009552 Genomic DNA. Translation: BAG00902.1.
AP009552 Genomic DNA. Translation: BAG05636.1.
RefSeqiWP_012264511.1. NC_010296.1.
YP_001656036.1. NC_010296.1.
YP_001656052.1. NC_010296.1.
YP_001656065.1. NC_010296.1.
YP_001656094.1. NC_010296.1.
YP_001660828.1. NC_010296.1.

3D structure databases

ProteinModelPortaliB0JIS8.
SMRiB0JIS8. Positions 10-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi449447.MAE_58140.

Proteomic databases

PaxDbiB0JIS8.
PRIDEiB0JIS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAG00844; BAG00844; MAE_10220.
BAG00860; BAG00860; MAE_10380.
BAG00873; BAG00873; MAE_10510.
BAG00902; BAG00902; MAE_10800.
BAG05636; BAG05636; MAE_58140.
GeneIDi5866658.
KEGGimar:MAE_10220.
mar:MAE_10380.
mar:MAE_10510.
mar:MAE_10800.
mar:MAE_58140.

Phylogenomic databases

eggNOGiNOG04871.
HOGENOMiHOG000246913.
KOiK02703.
OMAiTWITSTE.
OrthoDBiEOG6Q2SGP.

Enzyme and pathway databases

BioCyciMAER449447:GHO8-1024-MONOMER.
MAER449447:GHO8-1040-MONOMER.
MAER449447:GHO8-1053-MONOMER.
MAER449447:GHO8-1082-MONOMER.
MAER449447:GHO8-5862-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: NIES-843.

Entry informationi

Entry nameiPSBA_MICAN
AccessioniPrimary (citable) accession number: B0JIS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 18, 2008
Last modified: May 27, 2015
This is version 53 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, Reference 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.