Reviewed, UniProtKB/Swiss-Prot Q5X154 (TPMT_LEGPA)

Names and origin

Protein names

Recommended name:
    Thiopurine S-methyltransferase
    EC=2.1.1.67
Alternative name(s):
    Thiopurine methyltransferase

Gene names

Name:	tpm
Ordered Locus Names:	lpp2892

Organism

Legionella pneumophila (strain Paris) [Complete proteome] [HAMAP]

Taxonomic identifier

297246 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	221 AA.
Sequence status	Complete.
Protein existence	Inferred 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 component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	thiopurine S-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 221	221	Thiopurine S-methyltransferase HAMAP MF_00812		PRO_0000220121
Sites
	Binding site	12	1	S-adenosyl-L-methionine By similarity
	Binding site	47	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	68	1	S-adenosyl-L-methionine By similarity
	Binding site	125	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5X154-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 5F6B0BC6EFD1D8DB	FASTA	221	25,302
	10 20 30 40 50 60 MNKGQYFWNE LWCEGRISFH KEEVNPDLIA YVSSLNIPAK GRVLVPLCGK SVDMLWLVRQ 70 80 90 100 110 120 GYHVVGIELV EKAILQFVQE HQITVRENTI GQAKQYFTDN LNLWVTDIFA LNSALIEPVD 130 140 150 160 170 180 AIYDRAALVA LPKKLRPAYV DICLKWLKPG GSILLKTLQY NQEKVQGPPY SVSPEEIALS 190 200 210 220 YQQCAKIELL KSQKRIQEPN DHLFNLGISE VNDYVWCIRK G

References

[1]

"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity." Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C. Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR628336 Genomic DNA. Translation: CAH14045.1.
RefSeq	YP_125194.1.
3D structure databases
SMR	Q5X154. Positions 6-220.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5X154.
Genome annotation databases
GeneID	3116845.
GenomeReviews	Gene locus lpp2892 in contig CR628336_GR.
KEGG	lpp:lpp2892.
Organism-specific databases
LegioList	lpp2892.
CMR	Search...
Phylogenomic databases
eggNOG	COG0500.
HOGENOM	HBG444929.
OMA	GKSLDMC.
Enzyme and pathway databases
BioCyc	LPNE297246:LPP2892-MONOMER.
Family and domain databases
HAMAP	MF_00812. Thiopur_methtran. [Tree]
InterPro	IPR008854. Thiopurine_S-MeTrfase. IPR016822. Thiopurine_S-MeTrfase_sub. [Graphical view]
Pfam	PF05724. TPMT. 1 hit. [Graphical view]
PIRSF	PIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TPMT_LEGPA

Accession

Primary (citable) accession number: Q5X154

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	November 23, 2004
Last modified:	January 19, 2010
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)