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Q9I011 (TPMT_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thiopurine S-methyltransferase

EC=2.1.1.67
Alternative name(s):
Thiopurine methyltransferase
Gene names
Name:tpm
Ordered Locus Names:PA2832
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cytoplasm By similarity HAMAP MF_00812.

Sequence similarities

Belongs to the methyltransferase superfamily. TPMT family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   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_0000220126

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

Sequences

Sequence LengthMass (Da)Tools
Q9I011 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 3AFA7067401ED998

FASTA21824,875
        10         20         30         40         50         60 
MQADFWHARW ANNQIGFHLD EINPYLMRHL SRLRLQAGEQ ILVPLCGKTL DLAWLAAQGL 

        70         80         90        100        110        120 
EVLGVELSEK AVSDFFEEHD LHPEIDQLDG FRRYRVAGIT LLQGDFFALQ AEHLAQCRAF 

       130        140        150        160        170        180 
YDRAALIALP PEMRERYAGH LQAVLPTRSL GLLVTIDYPQ AEMAGPPFAV PDEEVRGYYA 

       190        200        210 
GGWRIEELER GDVLGVNWKF LERGVSWLDE AVYLLERG 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG06220.1.
PIRA83291.
RefSeqNP_251522.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9I011.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID882816.
GenomeReviewsGene locus PA2832 in contig AE004091_GR.
KEGGpae:PA2832.
NMPDRfig|208964.1.peg.2832.
PATRIC19840197. VBIPseAer58763_2969.

Organism-specific databases

PseudoCAPPA2832.

Phylogenomic databases

HOGENOMHBG444929.
OMAQGDIFTL.
ProtClustDBPRK13255.

Enzyme and pathway databases

BioCycPAER208964:PA2832-MONOMER.

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]
KOK00569.
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_PSEAE
AccessionPrimary (citable) accession number: Q9I011
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families