O86262 (TPMT_PSESJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiopurine S-methyltransferase
EC=2.1.1.67

Alternative name(s):
Tellurite-resistance determinant
Short name=TEL-R determinant
Thiopurine methyltransferase

Gene names

Name:

tpm

Organism

Pseudomonas syringae pv. pisi

Taxonomic identifier

59510 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas syringae

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biological cycling of tellurium and selenium. Tellurium resistance (Ter) mechanism. HAMAP MF_00812
Catalytic activity	S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. HAMAP MF_00812
Subcellular location	Cytoplasm HAMAP MF_00812.
Sequence similarities	Belongs to the methyltransferase superfamily. TPMT family.

Ontologies

Keywords
Biological process	Tellurium resistance
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	response to tellurium ion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	thiopurine S-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 218

218

Thiopurine S-methyltransferase HAMAP MF_00812

PRO_0000220129

Sites

Binding site

10

1

S-adenosyl-L-methionine By similarity

Binding site

45

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Binding site

66

1

S-adenosyl-L-methionine By similarity

Binding site

123

1

S-adenosyl-L-methionine By similarity

Secondary structure

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218

Helix Strand Turn

Details...

Beta strand

20 – 22

3

Helix

24 – 33

10

Beta strand

40 – 43

4

Turn

44 – 46

3

Helix

50 – 58

9

Beta strand

61 – 67

7

Helix

69 – 79

11

Beta strand

83 – 88

6

Beta strand

91 – 95

5

Beta strand

97 – 104

8

Beta strand

107 – 109

3

Helix

111 – 115

5

Beta strand

116 – 124

9

Helix

126 – 128

3

Helix

131 – 144

14

Beta strand

147 – 158

12

Beta strand

160 – 165

6

Helix

172 – 177

6

Beta strand

181 – 192

12

Turn

194 – 196

3

Helix

198 – 203

6

Beta strand

210 – 217

8

Sequences

	Sequence		Length	Mass (Da)
	O86262 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 5CD188EA5F9D171F	FASTA	218	24,446
	10 20 30 40 50 60 MKADFWLQRW SAGQIGFHQS EVNKDLQQYW SSLNVVPGAR VLVPLCGKSQ DMSWLSGQGY 70 80 90 100 110 120 HVVGAELSEA AVERYFTERG EQPHITSQGD FKVYAAPGIE IWCGDFFALT ARDIGHCAAF 130 140 150 160 170 180 YDRAAMIALP ADMRERYVQH LEALMPQACS GLLITLEYDQ ALLEGPPFSV PQTWLHRVMS 190 200 210 GNWEVTKVGG QDTLHSSARG LKAGLERMDE HVYVLERV

References

[1]	"A tellurite-resistance genetic determinant from phytopathogenic pseudomonads encodes a thiopurine methyltransferase: evidence of a widely-conserved family of methyltransferases." Cournoyer B., Watanabe S., Vivian A. Biochim. Biophys. Acta 1397:161-168(1998) [PubMed: 9565678] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Tertiary structure of thiopurine methyltransferase from Pseudomonas syringae, a bacterial orthologue of a polymorphic, drug-metabolizing enzyme." Scheuermann T.H., Lolis E., Hodsdon M.E. J. Mol. Biol. 333:573-585(2003) [PubMed: 14556746] [Abstract] Cited for: STRUCTURE BY NMR OF 18-218.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L49178 Genomic DNA. Translation: AAC27664.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PJZ	NMR	-	A	18-218	[»]

ProteinModelPortal

O86262.

SMR

O86262. Positions 18-218.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_00812. Thiopur_methtran.
[Tree]

InterPro

IPR022474. Thiopur_S-MeTfrase_Se/Te_detox.
IPR008854. Thiopurine_S-MeTrfase.
IPR016822. Thiopurine_S-MeTrfase_sub.
[Graphical view]

PANTHER

PTHR10259. PTHR10259. 1 hit.

Pfam

PF05724. TPMT. 1 hit.
[Graphical view]

PIRSF

PIRSF023956. Thiopurine_S-methyltransferase. 1 hit.

TIGRFAMs

TIGR03840. TMPT_Se_Te. 1 hit.

ProtoNet

Search...

Entry information

Entry name

TPMT_PSESJ

Accession

Primary (citable) accession number: O86262

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1998
Last modified:	October 19, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program