Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

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

Summary:
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 [Liu00].

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 [Liu00]. 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 [Liu00]; 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 , PDB:Structure:2XVA , PDB:Structure:2XVM , Pfam:IN-FAMILY:PF03848

Gene-Reaction Schematic: ?

GO Terms:

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

MultiFun Terms: cell processes protection drug resistance/sensitivity

Credits:
Created in EcoCyc 01-Dec-2010 by Keseler I , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: tellurite methyltransferase

EC Number: 2.1.1.265

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 Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Sequence Features

Feature Class Location Citations Comment
Mutagenesis-Variant 36
[Liu00, UniProt11]
Alternate sequence: N; UniProt: Loss of tellurite resistance.
Alternate sequence: A; UniProt: Loss of tellurite resistance.
Amino-Acid-Sites-That-Bind 38
[UniProt13]
UniProt: S-adenosyl-L-methionine; via carbonyl oxygen.
Amino-Acid-Sites-That-Bind 43
[UniProt13]
UniProt: S-adenosyl-L-methionine.
Amino-Acid-Sites-That-Bind 59
[UniProt13]
UniProt: S-adenosyl-L-methionine.
Mutagenesis-Variant 59
[Liu00, UniProt11]
Alternate sequence: A; UniProt: Loss of tellurite resistance.
Protein-Segment 86 -> 87
[UniProt13]
UniProt: S-adenosyl-L-methionine; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 96
[Liu00, UniProt11]
Alternate sequence: A; UniProt: Decrease in tellurite resistance.
Mutagenesis-Variant 97
[Liu00, UniProt11]
Alternate sequence: N; UniProt: Decrease in tellurite resistance.
Alternate sequence: E; UniProt: No effect on tellurite resistance.
Mutagenesis-Variant 98
[Liu00, UniProt11]
Alternate sequence: Y; UniProt: Loss of tellurite resistance.
Alternate sequence: A; UniProt: Loss of tellurite resistance.
Amino-Acid-Sites-That-Bind 102
[UniProt13]
UniProt: S-adenosyl-L-methionine.
Mutagenesis-Variant 176
[Choudhury11, UniProt13]
Alternate sequence: A; UniProt: 95% of wild-type methyltransferase activity on tellurite.
Mutagenesis-Variant 177
[Choudhury11, UniProt13]
Alternate sequence: A; UniProt: 35% of wild-type methyltransferase activity on tellurite.
Amino-Acid-Sites-That-Bind 177
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: probable.
Mutagenesis-Variant 184
[Choudhury11, UniProt13]
Alternate sequence: A; UniProt: 74% of wild-type methyltransferase activity on tellurite.

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


References

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

Liu00: 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

UniProt11: 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.

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

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, BIOCYC13A.