P0A6V5 · GLPE_ECOLI

Function

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.

Miscellaneous

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

Catalytic activity

Features

Showing features for active site.

1108102030405060708090100
TypeIDPosition(s)Description
Active site65Cysteine persulfide intermediate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionthiosulfate sulfurtransferase activity
Biological Processglycerol metabolic process
Biological Processsulfur utilization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thiosulfate sulfurtransferase GlpE
  • EC number

Gene names

    • Name
      glpE
    • Ordered locus names
      b3425, JW3388

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0A6V5
  • Secondary accessions
    • P09390
    • Q2M789
    • Q47235

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002005491-108Thiosulfate sulfurtransferase GlpE

Proteomic databases

Expression

Induction

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

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain17-105Rhodanese

Sequence similarities

Belongs to the GlpE family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    108
  • Mass (Da)
    12,082
  • Last updated
    2005-03-29 v1
  • Checksum
    18D5B461C2A8EF19
MDQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRDNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDVVYSIDGGFEAWQRQFPAEVAYGA

Sequence caution

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

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict108in Ref. 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M96795
EMBL· GenBank· DDBJ
AAC28165.1
EMBL· GenBank· DDBJ
Genomic DNA
X07520
EMBL· GenBank· DDBJ
CAA30397.1
EMBL· GenBank· DDBJ
Genomic DNA
M54940
EMBL· GenBank· DDBJ
AAA23889.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
U18997
EMBL· GenBank· DDBJ
AAA58223.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76450.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77867.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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