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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)DescriptionActionsGraphical viewLength
    Binding sitei26Glutathione 21 Publication1
    Binding sitei87Glutathione 11 Publication1
    Binding sitei101Glutathione 1; via amide nitrogen and carbonyl oxygen1 Publication1
    Binding sitei151Glutathione 11 Publication1
    Binding sitei178Glutathione 21 Publication1

    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.

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00001860171 – 288Disulfide-bond oxidoreductase YghUAdd BLAST288

    Proteomic databases

    EPDiQ46845.
    PaxDbiQ46845.
    PRIDEiQ46845.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1288
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni21 – 25Combined sources5
    Beta strandi42 – 49Combined sources8
    Helixi53 – 67Combined sources15
    Helixi71 – 73Combined sources3
    Beta strandi75 – 79Combined sources5
    Helixi82 – 84Combined sources3
    Helixi86 – 88Combined sources3
    Helixi90 – 95Combined sources6
    Beta strandi103 – 106Combined sources4
    Beta strandi109 – 111Combined sources3
    Beta strandi113 – 117Combined sources5
    Helixi118 – 129Combined sources12
    Helixi137 – 159Combined sources23
    Helixi161 – 166Combined sources6
    Helixi173 – 194Combined sources22
    Beta strandi202 – 204Combined sources3
    Helixi207 – 212Combined sources6
    Turni213 – 215Combined sources3
    Helixi216 – 221Combined sources6
    Turni228 – 232Combined sources5
    Helixi233 – 235Combined sources3
    Helixi237 – 247Combined sources11
    Helixi250 – 255Combined sources6
    Helixi265 – 267Combined sources3
    Beta strandi272 – 274Combined sources3
    Helixi277 – 280Combined sources4
    Helixi283 – 285Combined sources3

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ46845.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini46 – 133GST N-terminalAdd BLAST88
    Domaini139 – 265GST C-terminalAdd BLAST127

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni52 – 54Glutathione 1 binding3
    Regioni117 – 118Glutathione 1 binding2

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3C8EX-ray1.50A/B1-288[»]
    ProteinModelPortaliQ46845.
    SMRiQ46845.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261179. 10 interactors.
    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.

    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: November 2, 2016
    This is version 107 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.