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Protein

Glutathione S-transferase YfcF

Gene

yfcF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits glutathione (GSH) S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Enzyme regulationi

GSH transferase activity is inhibited by S-hexyl glutathione.1 Publication

Kineticsi

kcat is 0.11 sec(-1) for the GSH transferase reaction with CDNB as substrate.

  1. KM=0.24 mM for glutathione1 Publication
  2. KM=1.1 mM for 1-chloro-2,4-dinitrobenzene1 Publication

    pH dependencei

    Activity decreases as pH is lowered from neutral to acidic.1 Publication

    GO - Molecular functioni

    • glutathione transferase activity Source: EcoCyc
    • peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    • response to hydrogen peroxide Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase, Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:G7193-MONOMER.
    ECOL316407:JW2298-MONOMER.
    MetaCyc:G7193-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase YfcF (EC:2.5.1.18)
    Gene namesi
    Name:yfcF
    Ordered Locus Names:b2301, JW2298
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14109. yfcF.

    Pathology & Biotechi

    Disruption phenotypei

    Deletion of yfcF decreases the resistance of the bacteria to hydrogen peroxide.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101S → A: Nearly no effect on GSH transferase activity. 1 Publication
    Mutagenesisi16 – 161S → G: 2% of wild-type GSH transferase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 214214Glutathione S-transferase YfcFPRO_0000186015Add
    BLAST

    Proteomic databases

    PaxDbiP77544.

    Interactioni

    Protein-protein interaction databases

    IntActiP77544. 3 interactions.
    STRINGi511145.b2301.

    Structurei

    Secondary structure

    1
    214
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 116Combined sources
    Helixi17 – 2913Combined sources
    Beta strandi34 – 385Combined sources
    Beta strandi61 – 644Combined sources
    Beta strandi67 – 715Combined sources
    Helixi72 – 8211Combined sources
    Turni85 – 873Combined sources
    Helixi96 – 11116Combined sources
    Helixi114 – 1196Combined sources
    Helixi123 – 1264Combined sources
    Helixi136 – 15217Combined sources
    Turni153 – 1553Combined sources
    Helixi166 – 17914Combined sources
    Turni180 – 1823Combined sources
    Helixi187 – 19711Combined sources
    Helixi200 – 21011Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BBYX-ray1.85A1-214[»]
    ProteinModelPortaliP77544.
    SMRiP77544. Positions 3-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP77544.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 8782GST N-terminalAdd
    BLAST
    Domaini95 – 214120GST C-terminalAdd
    BLAST

    Sequence similaritiesi

    Belongs to the GST superfamily.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000255229.
    InParanoidiP77544.
    OMAiFSPYVMS.
    OrthoDBiEOG6R5C65.
    PhylomeDBiP77544.

    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]
    PfamiPF13417. GST_N_3. 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.

    P77544-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKPAITLWS DAHFFSPYVL SAWVALQEKG LSFHIKTIDL DSGEHLQPTW
    60 70 80 90 100
    QGYGQTRRVP LLQIDDFELS ESSAIAEYLE DRFAPPTWER IYPLDLENRA
    110 120 130 140 150
    RARQIQAWLR SDLMPIREER PTDVVFAGAK KAPLTAEGKA SAEKLFAMAE
    160 170 180 190 200
    HLLVLGQPNL FGEWCIADTD LALMINRLVL HGDEVPERLV DYATFQWQRA
    210
    SVQRFIALSA KQSG
    Length:214
    Mass (Da):24,326
    Last modified:February 1, 1997 - v1
    Checksum:i6B2308D403DA3077
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75361.1.
    AP009048 Genomic DNA. Translation: BAA16138.1.
    PIRiC65002.
    RefSeqiNP_416804.1. NC_000913.3.
    WP_000042442.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75361; AAC75361; b2301.
    BAA16138; BAA16138; BAA16138.
    GeneIDi946749.
    KEGGieco:b2301.
    PATRICi32119973. VBIEscCol129921_2396.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75361.1.
    AP009048 Genomic DNA. Translation: BAA16138.1.
    PIRiC65002.
    RefSeqiNP_416804.1. NC_000913.3.
    WP_000042442.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BBYX-ray1.85A1-214[»]
    ProteinModelPortaliP77544.
    SMRiP77544. Positions 3-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP77544. 3 interactions.
    STRINGi511145.b2301.

    Proteomic databases

    PaxDbiP77544.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75361; AAC75361; b2301.
    BAA16138; BAA16138; BAA16138.
    GeneIDi946749.
    KEGGieco:b2301.
    PATRICi32119973. VBIEscCol129921_2396.

    Organism-specific databases

    EchoBASEiEB3862.
    EcoGeneiEG14109. yfcF.

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000255229.
    InParanoidiP77544.
    OMAiFSPYVMS.
    OrthoDBiEOG6R5C65.
    PhylomeDBiP77544.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7193-MONOMER.
    ECOL316407:JW2298-MONOMER.
    MetaCyc:G7193-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP77544.
    PROiP77544.

    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]
    PfamiPF13417. GST_N_3. 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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress."
      Kanai T., Takahashi K., Inoue H.
      J. Biochem. 140:703-711(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEFENSE AGAINST OXIDATIVE STRESS, GSH TRANSFERASE ACTIVITY, PEROXIDASE ACTIVITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-10 AND SER-16.
      Strain: K12.
    5. "Crystal structure of glutathione S-transferase (NP_416804.1) from Escherichia coli K12 at 1.85 A resolution."
      Joint center for structural genomics (JCSG)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
      Strain: K12.

    Entry informationi

    Entry nameiYFCF_ECOLI
    AccessioniPrimary (citable) accession number: P77544
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: July 22, 2015
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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

    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 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.