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Protein

Thiopurine S-methyltransferase

Gene

tpm

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
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 sitei16 – 161S-adenosyl-L-methionineUniRule annotation
Binding sitei51 – 511S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
Binding sitei72 – 721S-adenosyl-L-methionineUniRule annotation
Binding sitei131 – 1311S-adenosyl-L-methionineUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciFTUL177416:GNBP-1701-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:FTT_1661
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 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 – 226226Thiopurine S-methyltransferasePRO_0000220119Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi177416.FTT_1661.

Structurei

3D structure databases

ProteinModelPortaliQ5NEH3.
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.
HOGENOMiHOG000262390.
KOiK00569.
OMAiPTWVETH.
OrthoDBiEOG6K3ZZV.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00812. Thiopur_methtran.
InterProiIPR029063. SAM-dependent_MTases.
IPR025835. Thiopurine_S-MeTrfase.
IPR008854. TPMT.
[Graphical view]
PfamiPF05724. TPMT. 1 hit.
[Graphical view]
PIRSFiPIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51585. SAM_MT_TPMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5NEH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKLETNNNQ YWLDRWQNDD VGFCQESPNE FLVKHFSKLN INDSSVCLIP
60 70 80 90 100
MCGCSIDMLF FLSKGVKVIG IELSEKAVLS FFSQNTINYE VIHGNDYKLY
110 120 130 140 150
KGDDIEIYVA DIFNLPKIAN NLPVFDIWYD RGAYIALPND LRTNYAKMML
160 170 180 190 200
EVCSNNTQIL LLVMEHDKKS QTPPYSVTQA ELIKNFSAKI KFELIDSKQR
210 220
DNIPDYRKAE GMTEQYYTTY LRKKQY
Length:226
Mass (Da):26,386
Last modified:February 1, 2005 - v1
Checksum:i640FFDD07F5E920C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG46294.1.
RefSeqiWP_003022610.1. NZ_CP010290.1.
YP_170569.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG46294; CAG46294; FTT_1661.
GeneIDi3190790.
KEGGiftu:FTT_1661.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG46294.1.
RefSeqiWP_003022610.1. NZ_CP010290.1.
YP_170569.1. NC_006570.2.

3D structure databases

ProteinModelPortaliQ5NEH3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi177416.FTT_1661.

Protocols and materials databases

DNASUi3190790.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG46294; CAG46294; FTT_1661.
GeneIDi3190790.
KEGGiftu:FTT_1661.

Phylogenomic databases

eggNOGiENOG4105FQ6. Bacteria.
ENOG4111GNF. LUCA.
HOGENOMiHOG000262390.
KOiK00569.
OMAiPTWVETH.
OrthoDBiEOG6K3ZZV.

Enzyme and pathway databases

BioCyciFTUL177416:GNBP-1701-MONOMER.

Family and domain databases

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

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SCHU S4 / Schu 4.

Entry informationi

Entry nameiTPMT_FRATT
AccessioniPrimary (citable) accession number: Q5NEH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: February 1, 2005
Last modified: November 11, 2015
This is version 67 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, Reference 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.