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Protein

Photosystem II protein D1

Gene

psbA

Organism
Heterocapsa triquetra (Dinoflagellate) (Glenodinium triquetrum)
Status
Reviewed-Annotation score: -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

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

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 bindingi122Magnesium (chlorophyll-a ChlzD1 axial ligand); via tele nitrogenUniRule annotation1
Binding sitei130Pheophytin D1UniRule annotation1
Sitei165Tyrosine radical intermediateUniRule annotation1
Metal bindingi174Calcium-manganese-oxide [Ca-4Mn-5O]; calciumUniRule annotation1
Metal bindingi174Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation1
Metal bindingi193Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation1
Sitei194Stabilizes free radical intermediateUniRule annotation1
Metal bindingi202Magnesium (chlorophyll-a PD1 axial ligand); via tele nitrogenUniRule annotation1
Metal bindingi219Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation1
Binding sitei219Quinone (B)UniRule annotation1
Metal bindingi276Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation1
Metal bindingi336Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; via tele nitrogenUniRule annotation1
Metal bindingi337Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3UniRule annotation1
Metal bindingi337Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation1
Metal bindingi346Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation1
Metal bindingi346Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2UniRule annotation1
Metal bindingi348Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via carboxylateUniRule annotation1
Metal bindingi348Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2; via carboxylateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Herbicide resistance, Photosynthesis, Transport
LigandCalcium, 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:psbAUniRule annotation
Encoded oniPlastid; Chloroplast
OrganismiHeterocapsa triquetra (Dinoflagellate) (Glenodinium triquetrum)
Taxonomic identifieri66468 [NCBI]
Taxonomic lineageiEukaryotaAlveolataDinophyceaePeridinialesHeterocapsaceaeHeterocapsa

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei33 – 50HelicalUniRule annotationAdd BLAST18
Transmembranei122 – 137HelicalUniRule annotationAdd BLAST16
Transmembranei146 – 160HelicalUniRule annotationAdd BLAST15
Transmembranei201 – 222HelicalUniRule annotationAdd BLAST22
Transmembranei278 – 292HelicalUniRule annotationAdd BLAST15

GO - Cellular componenti

Keywords - Cellular componenti

Chloroplast, Membrane, Photosystem II, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003164991 – 348Photosystem II protein D1UniRule annotationAdd BLAST348

Post-translational modificationi

Tyr-165 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.UniRule annotation

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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9XQV1
SMRiQ9XQV1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni268 – 269Quinone (B)UniRule annotation2

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.85.10, 1 hit
HAMAPiMF_01379 PSII_PsbA_D1, 1 hit
InterProiView protein in InterPro
IPR036854 Photo_II_D1/D2_sf
IPR000484 Photo_RC_L/M
IPR005867 PSII_D1
PANTHERiPTHR33149 PTHR33149, 1 hit
PfamiView protein in Pfam
PF00124 Photo_RC, 1 hit
SUPFAMiSSF81483 SSF81483, 1 hit
TIGRFAMsiTIGR01151 psbA, 1 hit
PROSITEiView protein in PROSITE
PS00244 REACTION_CENTER, 1 hit

Sequencei

Sequence statusi: Complete.

Q9XQV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNTFNTSNV FASAYSFWGS FIGFILSTSN RLYIGWFGIL MFPLLVLATV
60 70 80 90 100
AYIAAFIFAP PVDIDGIREP VAGALLYGNN IISGAVIPSS NAIGVHFYPV
110 120 130 140 150
WEALGFDEWL YNGGTYQFVV LHFIFGAGAY MGREWEFSFR LGMRPWIFVA
160 170 180 190 200
FSAPLVAASA VFIVYPIGQG SFSDGMPLGI SGTFNFMLVF QAEHNILMHP
210 220 230 240 250
FHILGVAAVF GGSLFSAMHG SLVTSSLLAE TAGDLSLNIG YNFGQEDETY
260 270 280 290 300
SISAAHGYFG RLIFQYASFN NSRSLHFFLA AWPVIGIWFT SLGVSTMAFN
310 320 330 340
LNGLNFNQSI IDSSGHLINS WADIVNRADL GMEVMHERNA HNFPLDLA
Length:348
Mass (Da):38,179
Last modified:November 1, 1999 - v1
Checksum:i8E005A9DAA07D46A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130033 Genomic DNA Translation: AAD44700.1
AB025587 Genomic DNA Translation: BAA83814.2

Similar proteinsi

Entry informationi

Entry nameiPSBA_HETTR
AccessioniPrimary (citable) accession number: Q9XQV1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 1, 1999
Last modified: February 28, 2018
This is version 82 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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