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Protein

Thiosulfate sulfurtransferase GlpE

Gene

glpE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 activityi

Thiosulfate + cyanide = sulfite + thiocyanate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei65Cysteine persulfide intermediateCurated1

GO - Molecular functioni

  • thiosulfate sulfurtransferase activity Source: EcoCyc

Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

BioCyciEcoCyc:EG10395-MONOMER
MetaCyc:EG10395-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase GlpE (EC:2.8.1.1)
Gene namesi
Name:glpE
Ordered Locus Names:b3425, JW3388
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10395 glpE

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002005491 – 108Thiosulfate sulfurtransferase GlpEAdd BLAST108

Proteomic databases

PaxDbiP0A6V5
PRIDEiP0A6V5

Expressioni

Inductioni

By infection by filamentous bacteriophages. Expression is positively regulated by cyclic AMP-cAMP receptor protein (cAMP-CRP).2 Publications

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4262487, 11 interactors
IntActiP0A6V5, 2 interactors
STRINGi316385.ECDH10B_3599

Structurei

Secondary structure

1108
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Helixi9 – 17Combined sources9
Beta strandi22 – 25Combined sources4
Helixi29 – 34Combined sources6
Helixi45 – 54Combined sources10
Beta strandi61 – 64Combined sources4
Beta strandi66 – 69Combined sources4
Helixi70 – 81Combined sources12
Beta strandi84 – 89Combined sources6
Helixi92 – 99Combined sources8
Helixi101 – 103Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GMXX-ray1.10A1-108[»]
1GN0X-ray1.80A1-108[»]
ProteinModelPortaliP0A6V5
SMRiP0A6V5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6V5

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 105RhodaneseAdd BLAST89

Sequence similaritiesi

Belongs to the GlpE family.Curated

Phylogenomic databases

eggNOGiENOG4105M78 Bacteria
COG0607 LUCA
HOGENOMiHOG000247776
InParanoidiP0A6V5
KOiK02439
OMAiVCYHGIS
PhylomeDBiP0A6V5

Family and domain databases

CDDicd01444 GlpE_ST, 1 hit
Gene3Di3.40.250.10, 1 hit
HAMAPiMF_01009 Thiosulf_sulfurtr, 1 hit
InterProiView protein in InterPro
IPR001763 Rhodanese-like_dom
IPR036873 Rhodanese-like_dom_sf
IPR023695 Thiosulf_sulfurTrfase
PfamiView protein in Pfam
PF00581 Rhodanese, 1 hit
SMARTiView protein in SMART
SM00450 RHOD, 1 hit
SUPFAMiSSF52821 SSF52821, 1 hit
PROSITEiView protein in PROSITE
PS50206 RHODANESE_3, 1 hit

Sequencei

Sequence statusi: Complete.

P0A6V5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQFECINVA DAHQKLQEKE AVLVDIRDPQ SFAMGHAVQA FHLTNDTLGA
60 70 80 90 100
FMRDNDFDTP VMVMCYHGNS SKGAAQYLLQ QGYDVVYSID GGFEAWQRQF

PAEVAYGA
Length:108
Mass (Da):12,082
Last modified:March 29, 2005 - v1
Checksum:i18D5B461C2A8EF19
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti108A → RNALYCPLLCGISDSNDVDD YLFC (PubMed:3045764).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiD65138 BVECGE
RefSeqiNP_417883.1, NC_000913.3
WP_000371928.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76450; AAC76450; b3425
BAE77867; BAE77867; BAE77867
GeneIDi947935
KEGGiecj:JW3388
eco:b3425
PATRICifig|511145.12.peg.3520

Similar proteinsi

Entry informationi

Entry nameiGLPE_ECOLI
AccessioniPrimary (citable) accession number: P0A6V5
Secondary accession number(s): P09390, Q2M789, Q47235
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: March 28, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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