Skip Header

Contribute Send feedback
Read comments (?) or add your own

O86262 (TPMT_PSESJ) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiopurine S-methyltransferase

EC=2.1.1.67
Alternative name(s):
Tellurite-resistance determinant
Short name=TEL-R determinant
Thiopurine methyltransferase
Gene names
Name:tpm
OrganismPseudomonas syringae pv. pisi
Taxonomic identifier59510 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas syringae

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biological cycling of tellurium and selenium. Tellurium resistance (Ter) mechanism. HAMAP MF_00812

Catalytic activity

S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. HAMAP MF_00812

Subcellular location

Cytoplasm HAMAP MF_00812.

Sequence similarities

Belongs to the methyltransferase superfamily. TPMT family.

Ontologies

Keywords
   Biological processTellurium resistance
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processresponse to tellurium ion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionthiopurine S-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 218218Thiopurine S-methyltransferase HAMAP MF_00812
PRO_0000220129

Sites

Binding site101S-adenosyl-L-methionine By similarity
Binding site451S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site661S-adenosyl-L-methionine By similarity
Binding site1231S-adenosyl-L-methionine By similarity

Secondary structure

........................................... 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O86262 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 5CD188EA5F9D171F

FASTA21824,446
        10         20         30         40         50         60 
MKADFWLQRW SAGQIGFHQS EVNKDLQQYW SSLNVVPGAR VLVPLCGKSQ DMSWLSGQGY 

        70         80         90        100        110        120 
HVVGAELSEA AVERYFTERG EQPHITSQGD FKVYAAPGIE IWCGDFFALT ARDIGHCAAF 

       130        140        150        160        170        180 
YDRAAMIALP ADMRERYVQH LEALMPQACS GLLITLEYDQ ALLEGPPFSV PQTWLHRVMS 

       190        200        210 
GNWEVTKVGG QDTLHSSARG LKAGLERMDE HVYVLERV 

« Hide

References

[1]"A tellurite-resistance genetic determinant from phytopathogenic pseudomonads encodes a thiopurine methyltransferase: evidence of a widely-conserved family of methyltransferases."
Cournoyer B., Watanabe S., Vivian A.
Biochim. Biophys. Acta 1397:161-168(1998) [PubMed: 9565678] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Tertiary structure of thiopurine methyltransferase from Pseudomonas syringae, a bacterial orthologue of a polymorphic, drug-metabolizing enzyme."
Scheuermann T.H., Lolis E., Hodsdon M.E.
J. Mol. Biol. 333:573-585(2003) [PubMed: 14556746] [Abstract]
Cited for: STRUCTURE BY NMR OF 18-218.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L49178 Genomic DNA. Translation: AAC27664.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PJZNMR-A18-218[»]
ProteinModelPortalO86262.
SMRO86262. Positions 18-218.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00812. Thiopur_methtran.
[Tree]
InterProIPR022474. Thiopur_S-MeTfrase_Se/Te_detox.
IPR008854. Thiopurine_S-MeTrfase.
IPR016822. Thiopurine_S-MeTrfase_sub.
[Graphical view]
PANTHERPTHR10259. PTHR10259. 1 hit.
PfamPF05724. TPMT. 1 hit.
[Graphical view]
PIRSFPIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
TIGRFAMsTIGR03840. TMPT_Se_Te. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTPMT_PSESJ
AccessionPrimary (citable) accession number: O86262
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: October 19, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families