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Protein

Thiopurine S-methyltransferase

Gene

tpm

Organism
Shewanella sp. (strain ANA-3)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101S-adenosyl-L-methionineUniRule annotation
Binding sitei45 – 451S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
Binding sitei66 – 661S-adenosyl-L-methionineUniRule annotation
Binding sitei123 – 1231S-adenosyl-L-methionineUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciSSP94122:GJ9K-601-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiopurine S-methyltransferaseUniRule annotation (EC:2.1.1.67UniRule annotation)
Alternative name(s):
Thiopurine methyltransferaseUniRule annotation
Gene namesi
Name:tpmUniRule annotation
Ordered Locus Names:Shewana3_0580
OrganismiShewanella sp. (strain ANA-3)
Taxonomic identifieri94122 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000002589 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Thiopurine S-methyltransferasePRO_1000047223Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA0KSQ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TPMT family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105FQ6. Bacteria.
ENOG4111GNF. LUCA.
HOGENOMiHOG000276919.
KOiK00569.
OMAiPTWVETH.
OrthoDBiEOG6K3ZZV.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00812. Thiopur_methtran.
InterProiIPR029063. SAM-dependent_MTases.
IPR022474. Thiopur_S-MeTfrase_Se/Te_detox.
IPR025835. Thiopurine_S-MeTrfase.
IPR008854. TPMT.
[Graphical view]
PfamiPF05724. TPMT. 1 hit.
[Graphical view]
PIRSFiPIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR03840. TMPT_Se_Te. 1 hit.
PROSITEiPS51585. SAM_MT_TPMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0KSQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPGFWHEKW QQQLIGFHQQ DINPFLVKYW HTLALPAGAQ VFVPLCGKSL
60 70 80 90 100
DMCFLAEQGH QVIGCELNEL AVQQFFEDNQ LPMQQSALGE HQHYHTEQVS
110 120 130 140 150
LYQGDIFTLP ASITGKVSGF YDRAALIAWP ESMRAQYAKQ LAQLLPQGSV
160 170 180 190 200
GLLVTLDYPQ EALSGPPFAV SPTWVETHLS DDFDIQLLDC QDVLADNPRF
210
VKKEVPWLNE AAYLLRRR
Length:218
Mass (Da):24,797
Last modified:December 12, 2006 - v1
Checksum:i31F96F2A3DECEFED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000469 Genomic DNA. Translation: ABK46819.1.
RefSeqiWP_011715775.1. NC_008577.1.

Genome annotation databases

EnsemblBacteriaiABK46819; ABK46819; Shewana3_0580.
KEGGishn:Shewana3_0580.
PATRICi23568744. VBISheSp134792_0832.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000469 Genomic DNA. Translation: ABK46819.1.
RefSeqiWP_011715775.1. NC_008577.1.

3D structure databases

ProteinModelPortaliA0KSQ0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK46819; ABK46819; Shewana3_0580.
KEGGishn:Shewana3_0580.
PATRICi23568744. VBISheSp134792_0832.

Phylogenomic databases

eggNOGiENOG4105FQ6. Bacteria.
ENOG4111GNF. LUCA.
HOGENOMiHOG000276919.
KOiK00569.
OMAiPTWVETH.
OrthoDBiEOG6K3ZZV.

Enzyme and pathway databases

BioCyciSSP94122:GJ9K-601-MONOMER.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00812. Thiopur_methtran.
InterProiIPR029063. SAM-dependent_MTases.
IPR022474. Thiopur_S-MeTfrase_Se/Te_detox.
IPR025835. Thiopurine_S-MeTrfase.
IPR008854. TPMT.
[Graphical view]
PfamiPF05724. TPMT. 1 hit.
[Graphical view]
PIRSFiPIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR03840. TMPT_Se_Te. 1 hit.
PROSITEiPS51585. SAM_MT_TPMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ANA-3.

Entry informationi

Entry nameiTPMT_SHESA
AccessioniPrimary (citable) accession number: A0KSQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: December 9, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.