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Protein

Disulfide-bond oxidoreductase YghU

Gene

yghU

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits a robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also displays a modest GSH-dependent peroxidase activity toward several organic hydroperoxides, such as cumene hydroperoxide and linoleic acid 13(S)-hydroperoxide, but does not reduce H2O2 or tert-butyl hydroperoxide at appreciable rates. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) with glutathionylspermidine (GspSH) as the nucleophilic substrate.1 Publication

Kineticsi

kcat is 74 sec(-1) for the disulfide-bond reductase reaction toward 2-hydroxyethyl disulfide. kcat is 0.050, 0.19 and 0.096 sec(-1) for the hydroperoxidase reaction with cumene hydroperoxide, linoleic acid 13(S)-hydroperoxide, and 15(S)-HpETE as substrate, respectively. kcat is 0.109 sec(-1) for the GSH transferase reaction with CDNB as substrate.

  1. KM=80 µM for glutathione (when assaying the GSH transferase activity with CDNB)1 Publication
  2. KM=1.1 mM for glutathione (when assaying the disulfide-bond reductase activity with 2-hydroxyethyl disulfide)1 Publication
  3. KM=16 µM for cumene hydroperoxide1 Publication
  4. KM=130 µM for linoleic acid 13(S)-hydroperoxide1 Publication
  5. KM=28 µM for 15(S)-HpETE1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei26 – 261Glutathione 21 Publication
    Binding sitei87 – 871Glutathione 11 Publication
    Binding sitei101 – 1011Glutathione 1; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei151 – 1511Glutathione 11 Publication
    Binding sitei178 – 1781Glutathione 21 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    BioCyciEcoCyc:G7553-MONOMER.
    ECOL316407:JW5492-MONOMER.
    MetaCyc:G7553-MONOMER.
    RETL1328306-WGS:GSTH-6938-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disulfide-bond oxidoreductase YghU (EC:1.8.4.-)
    Alternative name(s):
    GSH-dependent disulfide-bond oxidoreductase YghU
    GST N2-2
    Organic hydroperoxidase (EC:1.11.1.-)
    Gene namesi
    Name:yghU
    Ordered Locus Names:b2989, JW5492
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13005. yghU.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 288288Disulfide-bond oxidoreductase YghUPRO_0000186017Add
    BLAST

    Proteomic databases

    EPDiQ46845.
    PaxDbiQ46845.
    PRIDEiQ46845.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4261179. 10 interactions.
    DIPiDIP-12212N.
    STRINGi511145.b2989.

    Structurei

    Secondary structure

    1
    288
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni21 – 255Combined sources
    Beta strandi42 – 498Combined sources
    Helixi53 – 6715Combined sources
    Helixi71 – 733Combined sources
    Beta strandi75 – 795Combined sources
    Helixi82 – 843Combined sources
    Helixi86 – 883Combined sources
    Helixi90 – 956Combined sources
    Beta strandi103 – 1064Combined sources
    Beta strandi109 – 1113Combined sources
    Beta strandi113 – 1175Combined sources
    Helixi118 – 12912Combined sources
    Helixi137 – 15923Combined sources
    Helixi161 – 1666Combined sources
    Helixi173 – 19422Combined sources
    Beta strandi202 – 2043Combined sources
    Helixi207 – 2126Combined sources
    Turni213 – 2153Combined sources
    Helixi216 – 2216Combined sources
    Turni228 – 2325Combined sources
    Helixi233 – 2353Combined sources
    Helixi237 – 24711Combined sources
    Helixi250 – 2556Combined sources
    Helixi265 – 2673Combined sources
    Beta strandi272 – 2743Combined sources
    Helixi277 – 2804Combined sources
    Helixi283 – 2853Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3C8EX-ray1.50A/B1-288[»]
    ProteinModelPortaliQ46845.
    SMRiQ46845. Positions 5-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ46845.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 13388GST N-terminalAdd
    BLAST
    Domaini139 – 265127GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 543Glutathione 1 binding
    Regioni117 – 1182Glutathione 1 binding

    Sequence similaritiesi

    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiENOG4105CYM. Bacteria.
    COG0625. LUCA.
    HOGENOMiHOG000125752.
    InParanoidiQ46845.
    KOiK11209.
    OMAiYVPPKVW.
    PhylomeDBiQ46845.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q46845-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDNTYQPAK VWTWDKSAGG AFANINRPVS GPTHEKTLPV GKHPLQLYSL
    60 70 80 90 100
    GTPNGQKVTI MLEELLALGV TGAEYDAWLI RIGDGDQFSS GFVEVNPNSK
    110 120 130 140 150
    IPALRDHTHN PPIRVFESGS ILLYLAEKFG YFLPQDLAKR TETMNWLFWL
    160 170 180 190 200
    QGAAPFLGGG FGHFYHYAPV KIEYAINRFT MEAKRLLDVL DKQLAQHKFV
    210 220 230 240 250
    AGDEYTIADM AIWPWFGNVV LGGVYDAAEF LDAGSYKHVQ RWAKEVGERP
    260 270 280
    AVKRGRIVNR TNGPLNEQLH ERHDASDFET NTEDKRQG
    Length:288
    Mass (Da):32,392
    Last modified:May 30, 2000 - v2
    Checksum:i799B17697A3C1C42
    GO

    Sequence cautioni

    The sequence AAA69156 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U28377 Genomic DNA. Translation: AAA69156.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76025.2.
    AP009048 Genomic DNA. Translation: BAE77050.1.
    RefSeqiNP_417463.4. NC_000913.3.
    WP_001295515.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76025; AAC76025; b2989.
    BAE77050; BAE77050; BAE77050.
    GeneIDi947472.
    KEGGiecj:JW5492.
    eco:b2989.
    PATRICi32121394. VBIEscCol129921_3084.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U28377 Genomic DNA. Translation: AAA69156.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76025.2.
    AP009048 Genomic DNA. Translation: BAE77050.1.
    RefSeqiNP_417463.4. NC_000913.3.
    WP_001295515.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3C8EX-ray1.50A/B1-288[»]
    ProteinModelPortaliQ46845.
    SMRiQ46845. Positions 5-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261179. 10 interactions.
    DIPiDIP-12212N.
    STRINGi511145.b2989.

    Proteomic databases

    EPDiQ46845.
    PaxDbiQ46845.
    PRIDEiQ46845.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76025; AAC76025; b2989.
    BAE77050; BAE77050; BAE77050.
    GeneIDi947472.
    KEGGiecj:JW5492.
    eco:b2989.
    PATRICi32121394. VBIEscCol129921_3084.

    Organism-specific databases

    EchoBASEiEB2827.
    EcoGeneiEG13005. yghU.

    Phylogenomic databases

    eggNOGiENOG4105CYM. Bacteria.
    COG0625. LUCA.
    HOGENOMiHOG000125752.
    InParanoidiQ46845.
    KOiK11209.
    OMAiYVPPKVW.
    PhylomeDBiQ46845.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7553-MONOMER.
    ECOL316407:JW5492-MONOMER.
    MetaCyc:G7553-MONOMER.
    RETL1328306-WGS:GSTH-6938-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ46845.
    PROiQ46845.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiYGHU_ECOLI
    AccessioniPrimary (citable) accession number: Q46845
    Secondary accession number(s): Q2M9K6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: September 7, 2016
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds two molecules of GSH in each active site; there is one tight and one weak binding site for GSH.

    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.