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P0A6V5 (GLPE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiosulfate sulfurtransferase GlpE

EC=2.8.1.1
Gene names
Name:glpE
Ordered Locus Names:b3425, JW3388
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate. Possible association with the metabolism of glycerol-phosphate remains to be elucidated. HAMAP-Rule MF_01009

Catalytic activity

Thiosulfate + cyanide = sulfite + thiocyanate. HAMAP-Rule MF_01009

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_01009.

Induction

By infection by filamentous bacteriophages. Expression is positively regulated by cyclic AMP-cAMP receptor protein (cAMP-CRP). Ref.5 Ref.7

Miscellaneous

Incubation of GlpE with the cysteine-specific modifying reagent DTNB resulted in a greater-than-90% loss of activity.

Sequence similarities

Belongs to the GlpE family.

Contains 1 rhodanese domain.

Sequence caution

The sequence AAA23889.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycerol metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: EcoCyc

   Molecular_functionthiosulfate sulfurtransferase activity

Inferred from direct assay Ref.6. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 108108Thiosulfate sulfurtransferase GlpE HAMAP-Rule MF_01009
PRO_0000200549

Regions

Domain17 – 10589Rhodanese

Sites

Active site651Cysteine persulfide intermediate Probable

Experimental info

Sequence conflict1081A → RNALYCPLLCGISDSNDVDD YLFC Ref.2

Secondary structure

...................... 108
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6V5 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: 18D5B461C2A8EF19

FASTA10812,082
        10         20         30         40         50         60 
MDQFECINVA DAHQKLQEKE AVLVDIRDPQ SFAMGHAVQA FHLTNDTLGA FMRDNDFDTP 

        70         80         90        100 
VMVMCYHGNS SKGAAQYLLQ QGYDVVYSID GGFEAWQRQF PAEVAYGA 

« Hide

References

« Hide 'large scale' references
[1]"Repressor for the sn-glycerol 3-phosphate regulon of Escherichia coli K-12: primary structure and identification of the DNA-binding domain."
Zeng G., Ye S., Larson T.J.
J. Bacteriol. 178:7080-7089(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Nucleotide sequence of the glpR gene encoding the repressor for the glycerol-3-phosphate regulon of Escherichia coli K12."
Choi Y.-L., Kawase S., Nishida T., Sakai H., Komano T., Kawamukai M., Utsumi R., Kohara Y., Akiyama K.
Nucleic Acids Res. 16:7732-7732(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Regulation of glpD and glpE gene expression by a cyclic AMP-cAMP receptor protein (cAMP-CRP) complex in Escherichia coli."
Choi Y.-L., Kawase S., Kawamukai M., Sakai H., Komano T.
Biochim. Biophys. Acta 1088:31-35(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin."
Ray W.K., Zeng G., Potters M.B., Mansuri A.M., Larson T.J.
J. Bacteriol. 182:2277-2284(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: BL21-DE3.
[7]"Biochemical and genetic characterization of pspE and glpE, two single-domain sulfurtransferases of Escherichia coli."
Cheng H., Donahue J.L., Battle S.E., Ray W.K., Larson T.J.
Open Microbiol. J. 2:18-28(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: K12 / MG1655 / ATCC 47076.
[8]"Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 A resolution diffraction: a preliminary report."
Bordo D., Larson T.J., Donahue J.L., Spallarossa A., Bolognesi M.
Acta Crystallogr. D 56:1691-1693(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS).
Strain: BL21-DE3.
[9]"Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily."
Spallarossa A., Donahue J.L., Larson T.J., Bolognesi M., Bordo D.
Structure 9:1117-1125(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS).
Strain: BL21-DE3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96795 Genomic DNA. Translation: AAC28165.1.
X07520 Genomic DNA. Translation: CAA30397.1.
M54940 Genomic DNA. Translation: AAA23889.1. Different initiation.
U18997 Genomic DNA. Translation: AAA58223.1.
U00096 Genomic DNA. Translation: AAC76450.1.
AP009048 Genomic DNA. Translation: BAE77867.1.
PIRBVECGE. D65138.
RefSeqNP_417883.1. NC_000913.3.
YP_492008.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GMXX-ray1.10A1-108[»]
1GN0X-ray1.80A1-108[»]
ProteinModelPortalP0A6V5.
SMRP0A6V5. Positions 1-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A6V5. 2 interactions.
STRING511145.b3425.

Proteomic databases

PaxDbP0A6V5.
PRIDEP0A6V5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76450; AAC76450; b3425.
BAE77867; BAE77867; BAE77867.
GeneID12933493.
947935.
KEGGecj:Y75_p3752.
eco:b3425.
PATRIC32122286. VBIEscCol129921_3520.

Organism-specific databases

EchoBASEEB0390.
EcoGeneEG10395. glpE.

Phylogenomic databases

eggNOGCOG0607.
HOGENOMHOG000247776.
KOK02439.
OMAFSAWHEA.
OrthoDBEOG68DD6K.
PhylomeDBP0A6V5.
ProtClustDBPRK00162.

Enzyme and pathway databases

BioCycEcoCyc:EG10395-MONOMER.
ECOL316407:JW3388-MONOMER.
MetaCyc:EG10395-MONOMER.

Gene expression databases

GenevestigatorP0A6V5.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
HAMAPMF_01009. Thiosulf_sulfurtr.
InterProIPR001763. Rhodanese-like_dom.
IPR023695. Thiosulf_sulfurTrfase.
[Graphical view]
PfamPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6V5.
PROP0A6V5.

Entry information

Entry nameGLPE_ECOLI
AccessionPrimary (citable) accession number: P0A6V5
Secondary accession number(s): P09390, Q2M789, Q47235
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene