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A7MVH9 (TPMT_VIBHB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:VIBHAR_02114
OrganismVibrio harveyi (strain ATCC BAA-1116 / BB120) [Complete proteome] [HAMAP]
Taxonomic identifier338187 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length216 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
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 – 216216Thiopurine S-methyltransferase HAMAP MF_00812
PRO_1000047227

Sites

Binding site111S-adenosyl-L-methionine By similarity
Binding site461S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site671S-adenosyl-L-methionine By similarity
Binding site1221S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7MVH9 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: D32511F45CBAB587

FASTA21624,825
        10         20         30         40         50         60 
MRDQEFWHNK WASNQIGFHL DDVNPLLPAF WQYTNPKRED TVLVPLCGKS EDLIWLATKH 

        70         80         90        100        110        120 
DEVQGVELSL IAVRAFFAEH FYTPTVTPVN GMHELYQFDE LSIYTGDFFT APVSKADIIY 

       130        140        150        160        170        180 
DRAALVALPK EMREEYANRV KQLLNPGGRI LLVTLNYPQD EMSGPPFSVP VEEIEQLFEG 

       190        200        210 
YKVTCLNVDQ ADENHPKIAK KGLSRFSEEV YLIESK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000789 Genomic DNA. Translation: ABU71079.1.
RefSeqYP_001445306.1. NC_009783.1.

3D structure databases

ProteinModelPortalA7MVH9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7MVH9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5554510.
GenomeReviewsGene locus VIBHAR_02114 in contig CP000789_GR.
KEGGvha:VIBHAR_02114.
NMPDRfig|338187.4.peg.1572.
PATRIC20130974. VBIVibHar24526_2028.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0500.
HOGENOMHBG444929.
OMAQGDIFTL.
ProtClustDBPRK13255.

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_VIBHB
AccessionPrimary (citable) accession number: A7MVH9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 2, 2007
Last modified: January 25, 2012
This is version 28 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