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P0A6V5

- GLPE_ECOLI

UniProt

P0A6V5 - GLPE_ECOLI

Protein

Thiosulfate sulfurtransferase GlpE

Gene

glpE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Cysteine persulfide intermediateCurated

    GO - Molecular functioni

    1. thiosulfate sulfurtransferase activity Source: EcoCyc

    GO - Biological processi

    1. glycerol metabolic process Source: UniProtKB-HAMAP

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10395. glpE.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 108108Thiosulfate sulfurtransferase GlpEPRO_0000200549Add
    BLAST

    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

    Gene expression databases

    GenevestigatoriP0A6V5.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    IntActiP0A6V5. 2 interactions.
    STRINGi511145.b3425.

    Structurei

    Secondary structure

    1
    108
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Helixi9 – 179
    Beta strandi22 – 254
    Helixi29 – 346
    Helixi45 – 5410
    Beta strandi61 – 644
    Beta strandi66 – 694
    Helixi70 – 8112
    Beta strandi84 – 896
    Helixi92 – 998
    Helixi101 – 1033

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GMXX-ray1.10A1-108[»]
    1GN0X-ray1.80A1-108[»]
    ProteinModelPortaliP0A6V5.
    SMRiP0A6V5. Positions 1-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6V5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 10589RhodaneseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the GlpE family.Curated
    Contains 1 rhodanese domain.Curated

    Phylogenomic databases

    eggNOGiCOG0607.
    HOGENOMiHOG000247776.
    KOiK02439.
    OMAiILVMCYH.
    OrthoDBiEOG68DD6K.
    PhylomeDBiP0A6V5.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    HAMAPiMF_01009. Thiosulf_sulfurtr.
    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

    MDQFECINVA DAHQKLQEKE AVLVDIRDPQ SFAMGHAVQA FHLTNDTLGA    50
    FMRDNDFDTP VMVMCYHGNS SKGAAQYLLQ QGYDVVYSID GGFEAWQRQF 100
    PAEVAYGA 108
    Length:108
    Mass (Da):12,082
    Last modified:March 29, 2005 - v1
    Checksum:i18D5B461C2A8EF19
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081A → RNALYCPLLCGISDSNDVDD YLFC(PubMed:3045764)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_492008.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76450; AAC76450; b3425.
    BAE77867; BAE77867; BAE77867.
    GeneIDi12933493.
    947935.
    KEGGiecj:Y75_p3752.
    eco:b3425.
    PATRICi32122286. VBIEscCol129921_3520.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi D65138. BVECGE.
    RefSeqi NP_417883.1. NC_000913.3.
    YP_492008.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GMX X-ray 1.10 A 1-108 [» ]
    1GN0 X-ray 1.80 A 1-108 [» ]
    ProteinModelPortali P0A6V5.
    SMRi P0A6V5. Positions 1-108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0A6V5. 2 interactions.
    STRINGi 511145.b3425.

    Proteomic databases

    PaxDbi P0A6V5.
    PRIDEi P0A6V5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76450 ; AAC76450 ; b3425 .
    BAE77867 ; BAE77867 ; BAE77867 .
    GeneIDi 12933493.
    947935.
    KEGGi ecj:Y75_p3752.
    eco:b3425.
    PATRICi 32122286. VBIEscCol129921_3520.

    Organism-specific databases

    EchoBASEi EB0390.
    EcoGenei EG10395. glpE.

    Phylogenomic databases

    eggNOGi COG0607.
    HOGENOMi HOG000247776.
    KOi K02439.
    OMAi ILVMCYH.
    OrthoDBi EOG68DD6K.
    PhylomeDBi P0A6V5.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10395-MONOMER.
    ECOL316407:JW3388-MONOMER.
    MetaCyc:EG10395-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A6V5.
    PROi P0A6V5.

    Gene expression databases

    Genevestigatori P0A6V5.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    HAMAPi MF_01009. Thiosulf_sulfurtr.
    InterProi IPR001763. Rhodanese-like_dom.
    IPR023695. Thiosulf_sulfurTrfase.
    [Graphical view ]
    Pfami PF00581. Rhodanese. 1 hit.
    [Graphical view ]
    SMARTi SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52821. SSF52821. 1 hit.
    PROSITEi PS50206. RHODANESE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    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: October 1, 2014
    This is version 78 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

    External Data

    Dasty 3