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Q6YXN7 (Q6YXN7_PHYPA) Unreviewed, UniProtKB/TrEMBL

Last modified November 16, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Photosystem Q(B) protein HAMAP MF_01379

EC=1.10.3.9 HAMAP MF_01379
Alternative name(s):
32 kDa thylakoid membrane protein HAMAP MF_01379
Photosystem II protein D1 HAMAP MF_01379
Gene names
Name:psbA HAMAP MF_01379 EMBL BAC85059.1
Encoded onPlastid; Chloroplast EMBL BAC85059.1
OrganismPhyscomitrella patens subsp. patens (Moss)
Taxonomic identifier145481 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This is one of the two reaction center proteins of photosystem II (PSII) By similarity. HAMAP MF_01379

Catalytic activity

2 H2O + 2 plastoquinone + 4 light = O2 + 2 plastoquinol. HAMAP MF_01379

Cofactor

The psbA/B heterodimer binds P680, the primary electron donor of PSII. It shares a non-heme iron and each subunit binds additional chlorophylls and pheophytin. PsbA provides most of the ligands for the Mn-cluster of the oxygen-evolving complex By similarity. HAMAP MF_01379

Subunit structure

The psbA/B heterodimer binds the P680 chlorophylls and subsequent electron acceptors. PSII consists of a core antenna complex that captures photons and an electron transfer chain that converts photonic excitation into a charge separation. PSII forms dimeric complexes By similarity. HAMAP MF_01379

Subcellular location

Plastidchloroplast thylakoid membrane; Multi-pass membrane protein By similarity HAMAP MF_01379.

Miscellaneous

Herbicides such as atrazine, BNT, diuron or ioxynil bind to Q(B) and block electron transport By similarity. HAMAP MF_01379

Sequence similarities

Belongs to the reaction center pufL/M/psbA/D family. HAMAP MF_01379 RuleBase RU004331

Ontologies

Keywords
   Biological processElectron transport HAMAP MF_01379 RuleBase RU004332
Herbicide resistance HAMAP MF_01379
Photosynthesis
Transport
   Cellular componentChloroplast EMBL BAC85059.1
Membrane
Photosystem II HAMAP MF_01379 RuleBase RU004332
Plastid
Thylakoid HAMAP MF_01379
   DomainTransmembrane
Transmembrane helix HAMAP MF_01379
   LigandIron HAMAP MF_01379 RuleBase RU004332
Metal-binding HAMAP MF_01379 RuleBase RU004332
   Molecular functionOxidoreductase HAMAP MF_01379
   PTMAcetylation HAMAP MF_01379
Phosphoprotein HAMAP MF_01379
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processphotosynthetic electron transport in photosystem II

Inferred from electronic annotation. Source: InterPro

response to herbicide

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

light-harvesting complex

Inferred from electronic annotation. Source: InterPro

photosystem II

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionelectron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: HAMAP

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide345 – 3539 By similarity HAMAP MF_01379

Regions

Transmembrane36 – 5621Helical; By similarity HAMAP MF_01379
Transmembrane109 – 12921Helical; By similarity HAMAP MF_01379
Transmembrane141 – 16424Helical; By similarity HAMAP MF_01379
Transmembrane192 – 21827Helical; By similarity HAMAP MF_01379
Transmembrane269 – 28921Helical; By similarity HAMAP MF_01379

Sites

Metal binding2151Iron; shared with heterodimeric partner By similarity HAMAP MF_01379
Metal binding2721Iron; shared with heterodimeric partner By similarity HAMAP MF_01379
Site344 – 3452Cleavage; by CtpA By similarity HAMAP MF_01379

Amino acid modifications

Modified residue21N-acetylthreonine By similarity HAMAP MF_01379
Modified residue21Phosphothreonine By similarity HAMAP MF_01379

Sequences

Sequence LengthMass (Da)Tools
Q6YXN7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9E6C1AD6A7CA193D

FASTA35338,811
        10         20         30         40         50         60 
MTATLERRES ASLWGRFCDW VTSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI 

        70         80         90        100        110        120 
DGIREPVSGS LLYGNNIISA AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL 

       130        140        150        160        170        180 
LGVACYMGRE WELSYRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF 

       190        200        210        220        230        240 
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANAGYKFG 

       250        260        270        280        290        300 
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF 

       310        320        330        340        350 
NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLASVEAPS VNG 

« Hide

References

[1]"Complete chloroplast DNA sequence of the moss Physcomitrella patens: evidence for the loss and relocation of rpoA from the chloroplast to the nucleus."
Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.
Nucleic Acids Res. 31:5324-5331(2003) [PubMed: 12954768] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP005672 Genomic DNA. Translation: BAC85059.1.
RefSeqNP_904209.1. NC_005087.1.

3D structure databases

ProteinModelPortalQ6YXN7.
SMRQ6YXN7. Positions 10-344.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2546772.
KEGGppp:PhpapaCp046.

Phylogenomic databases

ProtClustDBCHL00003.

Family and domain databases

HAMAPMF_01379. PSII_PsbA_D1.
[Tree]
InterProIPR000484. Photo_RC_L/M.
IPR005867. PSII_PsbA/D1.
[Graphical view]
Gene3DG3DSA:1.20.85.10. Photo_RC_L/M. 1 hit.
KOK02703.
PfamPF00124. Photo_RC. 1 hit.
[Graphical view]
PRINTSPR00256. REACTNCENTRE.
SUPFAMSSF81483. Photo_RC_L/M. 1 hit.
TIGRFAMsTIGR01151. PsbA. 1 hit.
PROSITEPS00244. REACTION_CENTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ6YXN7_PHYPA
AccessionPrimary (citable) accession number: Q6YXN7
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: November 16, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)