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Protein

Thiosulfate sulfurtransferase GlpE

Gene

glpE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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.

Catalytic activityi

Thiosulfate + cyanide = sulfite + thiocyanate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei65Cysteine persulfide intermediateCurated1

GO - Molecular functioni

  • thiosulfate sulfurtransferase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciEcoCyc:EG10395-MONOMER.
ECOL316407:JW3388-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
Complete GO annotation...

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.
STRINGi511145.b3425.

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
Contains 1 rhodanese domain.Curated

Phylogenomic databases

eggNOGiENOG4105M78. Bacteria.
COG0607. LUCA.
HOGENOMiHOG000247776.
InParanoidiP0A6V5.
KOiK02439.
OMAiMDQFQHI.
PhylomeDBiP0A6V5.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
HAMAPiMF_01009. Thiosulf_sulfurtr. 1 hit.
InterProiIPR001763. Rhodanese-like_dom.
IPR023695. Thiosulf_sulfurTrfase.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

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.
PATRICi32122286. VBIEscCol129921_3520.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi4262487. 11 interactors.
IntActiP0A6V5. 2 interactors.
STRINGi511145.b3425.

Proteomic databases

PaxDbiP0A6V5.
PRIDEiP0A6V5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76450; AAC76450; b3425.
BAE77867; BAE77867; BAE77867.
GeneIDi947935.
KEGGiecj:JW3388.
eco:b3425.
PATRICi32122286. VBIEscCol129921_3520.

Organism-specific databases

EchoBASEiEB0390.
EcoGeneiEG10395. glpE.

Phylogenomic databases

eggNOGiENOG4105M78. Bacteria.
COG0607. LUCA.
HOGENOMiHOG000247776.
InParanoidiP0A6V5.
KOiK02439.
OMAiMDQFQHI.
PhylomeDBiP0A6V5.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A6V5.
PROiP0A6V5.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
HAMAPiMF_01009. Thiosulf_sulfurtr. 1 hit.
InterProiIPR001763. Rhodanese-like_dom.
IPR023695. Thiosulf_sulfurTrfase.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLPE_ECOLI
AccessioniPrimary (citable) accession number: P0A6V5
Secondary accession number(s): P09390, Q2M789, Q47235
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.