Escherichia coli K-12 substr. MG1655 Enzyme: thiosulfate sulfurtransferase

Gene: glpE Accession Numbers: EG10395 (EcoCyc), b3425, ECK3411

Regulation Summary Diagram: ?

Regulation summary diagram for glpE

Subunit composition of thiosulfate sulfurtransferase = [GlpE]2

GlpE is a sulfurtransferase of the rhodanese family that catalyzes the transfer of sulfur from thiosulfate to a recipient compound such as thioredoxin or cyanide, with thioredoxin thought to be the likely in vivo substrate [Ray00]. The role of GlpE in the cell is still unknown.

Based on analysis of deletion mutants, GlpE appears to carry out about 10% of the thiosulfate sulfurtransferase activity, with PspE accounting for approximately 85% [Cheng08a]. Enzymatic activity requires at least one of the protein's cysteine residues; the reaction likely proceeds via an enzyme-sulfur intermediate utilizing a double-displacement mechanism [Ray00].

A crystal structure of GlpE has been determined to 1.06 Å resolution [Spallarossa01, Bordo00]. In contrast to results from native gel chromatography [Ray00], GlpE is monomeric in the crystal structure [Spallarossa01]. Cys65, the expected catalytic residue, is persulfurated in the crystal structure [Spallarossa01]. NMR resonance assignments have been reported [Li11b].

Expression of glpE is positively regulated by cAMP-CRP [Choi91].

Gene Citations: [Zeng96]

Locations: cytosol

Map Position: [3,559,520 <- 3,559,846] (76.72 centisomes, 276°)
Length: 327 bp / 108 aa

Molecular Weight of Polypeptide: 12.082 kD (from nucleotide sequence), 13.0 kD (experimental) [Schweizer86 ]

Molecular Weight of Multimer: 22.5 kD (experimental) [Ray00]

Unification Links: ASAP:ABE-0011182 , CGSC:18265 , EchoBASE:EB0390 , EcoGene:EG10395 , EcoliWiki:b3425 , ModBase:P0A6V5 , OU-Microarray:b3425 , PortEco:glpE , PR:PRO_000022796 , Pride:P0A6V5 , Protein Model Portal:P0A6V5 , RefSeq:NP_417883 , RegulonDB:EG10395 , SMR:P0A6V5 , String:511145.b3425 , UniProt:P0A6V5

Relationship Links: InterPro:IN-FAMILY:IPR001763 , InterPro:IN-FAMILY:IPR023695 , PDB:Structure:1GMX , PDB:Structure:1GN0 , Pfam:IN-FAMILY:PF00581 , Prosite:IN-FAMILY:PS50206 , Smart:IN-FAMILY:SM00450

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for glpE

GO Terms:

Biological Process: GO:0006071 - glycerol metabolic process Inferred by computational analysis [GOA06]
Molecular Function: GO:0004792 - thiosulfate sulfurtransferase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Ray00]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a, Ray00]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ray00]


Essentiality data for glpE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
Yes [Feist07, Comment 3]

Curated 17-Dec-2009 by Shearer A , SRI International
Last-Curated ? 13-Dec-2011 by Keseler I , SRI International

Enzymatic reaction of: thiosulfate sulfurtransferase

EC Number: 2.8.1.-

a reduced thioredoxin + thiosulfate <=> an oxidized thioredoxin + sulfite + hydrogen sulfide + H+

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.

Reversibility of this reaction is unspecified.

Activity was assayed with thioredoxin 1 [Ray00].

Kinetic Parameters:

Km (μM)
a reduced thioredoxin

Enzymatic reaction of: thiosulfate sulfurtransferase

Synonyms: rhodanese, thiosulfate cyanide transsulfurase, thiosulfate thiotransferase, thiosulfate:cyanide sulfurtransferase

EC Number:

hydrogen cyanide + thiosulfate <=> thiocyanate + sulfite + 2 H+

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 favored in the direction shown.

In Pathways: thiosulfate disproportionation III (rhodanese)

The enzyme shows substrate inhibition by thiosulfate at low concentrations of cyanate [Ray00].

Kinetic Parameters:

Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
hydrogen cyanide

Sequence Features

Protein sequence of GlpE with features indicated

Feature Class Location Citations Comment
Conserved-Region 17 -> 105
UniProt: Rhodanese;
Active-Site 65
UniProt: Cysteine persulfide intermediate; Non-Experimental Qualifier: probable;
Sequence-Conflict 108
[Choi88, UniProt10]
UniProt: (in Ref. 2);

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b3425 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10395; confirmed by SwissProt match.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bordo00: Bordo D, Larson TJ, Donahue JL, Spallarossa A, Bolognesi M (2000). "Crystals of GlpE, a 12 kDa sulfurtransferase from escherichia coli, display 1.06 A resolution diffraction: a preliminary report." Acta Crystallogr D Biol Crystallogr 56(Pt 12);1691-3. PMID: 11092948

Cheng08a: Cheng H, Donahue JL, Battle SE, Ray WK, Larson TJ (2008). "Biochemical and Genetic Characterization of PspE and GlpE, Two Single-domain Sulfurtransferases of Escherichia coli." Open Microbiol J 2;18-28. PMID: 19088907

Choi88: Choi YL, Kawase S, Nishida T, Sakai H, Komano T, Kawamukai M, Utsumi R, Kohara Y, Akiyama K (1988). "Nucleotide sequence of the glpR gene encoding the repressor for the glycerol-3-phosphate regulon of Escherichia coli K12." Nucleic Acids Res 16(15);7732. PMID: 3045764

Choi91: Choi YL, Kawase S, Kawamukai M, Sakai H, Komano T (1991). "Regulation of glpD and glpE gene expression by a cyclic AMP-cAMP receptor protein (cAMP-CRP) complex in Escherichia coli." Biochim Biophys Acta 1991;1088(1);31-5. PMID: 1846566

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

Dyson90: Dyson HJ, Gippert GP, Case DA, Holmgren A, Wright PE (1990). "Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy." Biochemistry 1990;29(17);4129-36. PMID: 2193685

Eklund84: Eklund H, Cambillau C, Sjoberg BM, Holmgren A, Jornvall H, Hoog JO, Branden CI (1984). "Conformational and functional similarities between glutaredoxin and thioredoxins." EMBO J 1984;3(7);1443-9. PMID: 6378624

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gleason88: Gleason FK, Holmgren A (1988). "Thioredoxin and related proteins in procaryotes." FEMS Microbiol Rev 1988;4(4);271-97. PMID: 3152490

Gleason90: Gleason FK, Lim CJ, Gerami-Nejad M, Fuchs JA (1990). "Characterization of Escherichia coli thioredoxins with altered active site residues." Biochemistry 1990;29(15);3701-9. PMID: 2187529

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Holmgren85: Holmgren A (1985). "Thioredoxin." Annu Rev Biochem 1985;54;237-71. PMID: 3896121

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Katti90: Katti SK, LeMaster DM, Eklund H (1990). "Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution." J Mol Biol 1990;212(1);167-84. PMID: 2181145

Li11b: Li H, Xia B, Jin C (2011). "1H, 13C and 15N resonance assignments of rhodanese GlpE from Escherichia coli." Biomol NMR Assign 5(1);97-9. PMID: 20960079

Nikkola93: Nikkola M, Gleason FK, Fuchs JA, Eklund H (1993). "Crystal structure analysis of a mutant Escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid." Biochemistry 1993;32(19);5093-8. PMID: 8098620

Ray00: Ray WK, Zeng G, Potters MB, Mansuri AM, Larson TJ (2000). "Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin." J Bacteriol 2000;182(8);2277-84. PMID: 10735872

Schweizer86: Schweizer H, Sweet G, Larson TJ (1986). "Physical and genetic structure of the glpD-malT interval of the Escherichia coli K-12 chromosome. Identification of two new structural genes of the glp-regulon." Mol Gen Genet 202(3);488-92. PMID: 3012272

Spallarossa01: Spallarossa A, Donahue JL, Larson TJ, Bolognesi M, Bordo D (2001). "Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily." Structure 9(11);1117-25. PMID: 11709175

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10b: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 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."

Zeng96: Zeng G, Ye S, Larson TJ (1996). "Repressor for the sn-glycerol 3-phosphate regulon of Escherichia coli K-12: primary structure and identification of the DNA-binding domain." J Bacteriol 1996;178(24);7080-9. PMID: 8955387

Other References Related to Gene Regulation

Weissenborn92: Weissenborn DL, Wittekindt N, Larson TJ (1992). "Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12." J Biol Chem 1992;267(9);6122-31. PMID: 1372899

Yang96c: Yang B, Larson TJ (1996). "Action at a distance for negative control of transcription of the glpD gene encoding sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12." J Bacteriol 178(24);7090-8. PMID: 8955388

Yang98b: Yang B, Larson TJ (1998). "Multiple promoters are responsible for transcription of the glpEGR operon of Escherichia coli K-12." Biochim Biophys Acta 1998;1396(1);114-26. PMID: 9524241

Ye88: Ye SZ, Larson TJ (1988). "Structures of the promoter and operator of the glpD gene encoding aerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12." J Bacteriol 1988;170(9);4209-15. PMID: 3045087

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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