MetaCyc Enzyme: tellurite methyltransferase

Gene: tehB Accession Numbers: EG11884 (MetaCyc), b1430, ECK1423

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of tellurite methyltransferase = [TehB]2
         tellurite methyltransferase = TehB

TehB was shown to have tellurite methyltransferase activity [Choudhury11]. TehB was earlier shown to cause a SAM-dependent loss of TeO32- from an assay mixture; the reaction product was unknown, but does not consist of a volatile form of methylated tellurium [Liu00a].

The TehB protein in conjunction with TehA confers resistance to tellurite when expressed on a multicopy plasmid [Turner95]. Sequence analysis of TehB showed the presence of conserved sequence motifs occurring in S-adenosylmethionine (SAM)-dependent non-nucleic acid methyltransferases, and site-directed mutagenesis of conserved residues cause loss of tellurite resistance [Liu00a]. Cysteine residues in TehB have also been shown to be involved in tellurite resistance [DyllickBrenzing00].

Dynamic light-scattering experiments show a conformational change upon addition of SAM and TeO32-, indicating that TehB binds both SAM and tellurite. Measurement of the hydrodynamic radius indicates that the protein is a dimer in solution [Liu00a]; the dimer form appears to be stabilized upon tellurite exposure [DyllickBrenzing00]. Crystal structures of TehB in the presence of the cofactor analogs SAH (1.48 Å resolution) and sinefungin (1.9 Å resolution) have been solved [Choudhury10, Choudhury11]. The active site Arg177 residue was predicted from the structures and confirmed by site-directed mutagenesis [Choudhury11].

Tellurite resistance conferred by tehAB is limited to growth in rich medium and is dependent on the presence of a functional electron transport chain and functional quinone pool in the cell [Turner95a].

Locations: cytosol

Map Position: [1,499,586 -> 1,500,179]

Molecular Weight of Polypeptide: 22.531 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0004772 , CGSC:32109 , DIP:DIP-10978N , EchoBASE:EB1830 , EcoGene:EG11884 , EcoliWiki:b1430 , Mint:MINT-1274665 , ModBase:P25397 , OU-Microarray:b1430 , PortEco:tehB , PR:PRO_000024047 , Protein Model Portal:P25397 , RefSeq:NP_415947 , RegulonDB:EG11884 , SMR:P25397 , String:511145.b1430 , UniProt:P25397

Relationship Links: InterPro:IN-FAMILY:IPR004537 , InterPro:IN-FAMILY:IPR015985 , InterPro:IN-FAMILY:IPR029063 , PDB:Structure:2XVA , PDB:Structure:2XVM , Pfam:IN-FAMILY:PF03848

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0046690 - response to tellurium ion Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01a, DyllickBrenzing00]
GO:0009636 - response to toxic substance Inferred by computational analysis [UniProtGOA11]
GO:0032259 - methylation Inferred by computational analysis [UniProtGOA11]
GO:0046677 - response to antibiotic Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0008757 - S-adenosylmethionine-dependent methyltransferase activity Inferred from experiment Inferred by computational analysis [GOA01a, Choudhury11]
GO:0008168 - methyltransferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA01a]

MultiFun Terms: cell processes protection drug resistance/sensitivity

Created in EcoCyc 01-Dec-2010 by Keseler I , SRI International
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Enzymatic reaction of: tellurite methyltransferase

EC Number:

tellurite + S-adenosyl-L-methionine <=> methanetelluronate + S-adenosyl-L-homocysteine

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Sequence Features

Feature Class Location Citations Comment
Mutagenesis-Variant 36
[Liu00a, UniProt11a]
A or N: Loss of tellurite resistance.
Amino-Acid-Sites-That-Bind 38
UniProt: S-adenosyl-L-methionine; via carbonyl oxygen.
Amino-Acid-Sites-That-Bind 43
UniProt: S-adenosyl-L-methionine.
Amino-Acid-Sites-That-Bind 59
UniProt: S-adenosyl-L-methionine.
Mutagenesis-Variant 59
[Liu00a, UniProt11a]
UniProt: Loss of tellurite resistance.
Protein-Segment 86 -> 87
UniProt: S-adenosyl-L-methionine; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 96
[Liu00a, UniProt11a]
UniProt: Decrease in tellurite resistance.
Mutagenesis-Variant 97
[Liu00a, UniProt11a]
[Liu00a, UniProt11a]
N: Decrease in tellurite resistance.
E: No effect on tellurite resistance.
Mutagenesis-Variant 98
[Liu00a, UniProt11a]
A or Y: Loss of tellurite resistance.
Amino-Acid-Sites-That-Bind 102
UniProt: S-adenosyl-L-methionine.
Mutagenesis-Variant 176
[Choudhury11, UniProt13]
UniProt: 95% of wild-type methyltransferase activity on tellurite.
Mutagenesis-Variant 177
[Choudhury11, UniProt13]
UniProt: 35% of wild-type methyltransferase activity on tellurite.
Amino-Acid-Sites-That-Bind 177
UniProt: Substrate; Non-Experimental Qualifier: probable.
Mutagenesis-Variant 184
[Choudhury11, UniProt13]
UniProt: 74% of wild-type methyltransferase activity on tellurite.

10/20/97 Gene b1430 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11884; confirmed by SwissProt match.


Choudhury10: Choudhury HG, Beis K (2010). "Crystallization and initial X-ray diffraction analysis of the tellurite-resistance S-adenosyl-L-methionine transferase protein TehB from Escherichia coli." Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 11);1496-9. PMID: 21045305

Choudhury11: Choudhury HG, Cameron AD, Iwata S, Beis K (2011). "Structure and mechanism of the chalcogen-detoxifying protein TehB from Escherichia coli." Biochem J 435(1);85-91. PMID: 21244361

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

DyllickBrenzing00: Dyllick-Brenzinger M, Liu M, Winstone TL, Taylor DE, Turner RJ (2000). "The role of cysteine residues in tellurite resistance mediated by the TehAB determinant." Biochem Biophys Res Commun 277(2);394-400. PMID: 11032735

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Liu00a: Liu M, Turner RJ, Winstone TL, Saetre A, Dyllick-Brenzinger M, Jickling G, Tari LW, Weiner JH, Taylor DE (2000). "Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance." J Bacteriol 182(22);6509-13. PMID: 11053398

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Turner95: Turner RJ, Weiner JH, Taylor DE (1995). "Neither reduced uptake nor increased efflux is encoded by tellurite resistance determinants expressed in Escherichia coli." Can J Microbiol 41(1);92-8. PMID: 7728659

Turner95a: Turner RJ, Weiner JH, Taylor DE (1995). "The tellurite-resistance determinants tehAtehB and klaAklaBtelB have different biochemical requirements." Microbiology 141 ( Pt 12);3133-40. PMID: 8574407

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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