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Q56415

- FOSA_SERMA

UniProt

Q56415 - FOSA_SERMA

Protein

Glutathione transferase FosA

Gene

fosA

Organism
Serratia marcescens
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin.1 Publication

    Catalytic activityi

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

    Cofactori

    Manganese.1 Publication

    Enzyme regulationi

    Requires the monovalent cation K+ for optimal activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi7 – 71Manganese
    Metal bindingi67 – 671Manganese
    Metal bindingi113 – 1131Manganese

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    Manganese, Metal-binding, Potassium

    Enzyme and pathway databases

    SABIO-RKQ56415.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione transferase FosA (EC:2.5.1.18)
    Alternative name(s):
    Fosfomycin resistance protein
    Gene namesi
    Name:fosA
    Synonyms:fos
    OrganismiSerratia marcescens
    Taxonomic identifieri615 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71H → A: Strong decrease in fosfomycin resistance. 1 Publication
    Mutagenesisi7 – 71H → Q: Decrease in fosfomycin resistance. 1 Publication
    Mutagenesisi67 – 671H → A: Loss of fosfomycin resistance. 1 Publication
    Mutagenesisi67 – 671H → Q: Decrease in fosfomycin resistance. 1 Publication
    Mutagenesisi113 – 1131E → A: Strong decrease in fosfomycin resistance. 1 Publication
    Mutagenesisi113 – 1131E → Q: Decrease in fosfomycin resistance. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 141141Glutathione transferase FosAPRO_0000164044Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    141
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1310
    Helixi15 – 239
    Beta strandi29 – 346
    Beta strandi37 – 426
    Beta strandi45 – 517
    Helixi60 – 623
    Beta strandi67 – 715
    Turni74 – 763
    Helixi77 – 8610
    Beta strandi91 – 933
    Beta strandi97 – 1059
    Beta strandi111 – 1166
    Helixi119 – 12810
    Beta strandi135 – 1373

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NPBX-ray2.50A/B/C/D/E/F1-141[»]
    ProteinModelPortaliQ56415.
    SMRiQ56415. Positions 1-140.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ56415.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.10.180.10. 1 hit.
    InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR004360. Glyas_Fos-R_dOase_dom.
    [Graphical view]
    PfamiPF00903. Glyoxalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF54593. SSF54593. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q56415-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLQSLNHLTL AVSDLQKSVT FWHELLGLTL HARWNTGAYL TCGDLWVCLS    50
    YDEARQYVPP QESDYTHYAF TVAEEDFEPL SQRLEQAGVT IWKQNKSEGA 100
    SFYFLDPDGH KLELHVGSLA ARLAACREKP YAGMVFTSDE A 141
    Length:141
    Mass (Da):15,959
    Last modified:November 1, 1996 - v1
    Checksum:i7BA4E5BF33FF3315
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85195 Genomic DNA. Translation: AAA98399.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85195 Genomic DNA. Translation: AAA98399.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NPB X-ray 2.50 A/B/C/D/E/F 1-141 [» ]
    ProteinModelPortali Q56415.
    SMRi Q56415. Positions 1-140.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK Q56415.

    Miscellaneous databases

    EvolutionaryTracei Q56415.

    Family and domain databases

    Gene3Di 3.10.180.10. 1 hit.
    InterProi IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR004360. Glyas_Fos-R_dOase_dom.
    [Graphical view ]
    Pfami PF00903. Glyoxalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54593. SSF54593. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and intracellular location of the product of the fosfomycin resistance gene from transposon Tn2921."
      Navas J., Leon J., Arroyo M., Garcia Lobo J.M.
      Antimicrob. Agents Chemother. 34:2016-2018(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
      Transposon: Tn2921.
    2. "Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases."
      Bernat B.A., Laughlin L.T., Armstrong R.N.
      Biochemistry 36:3050-3055(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, SUBUNIT.
    3. "Elucidation of a monovalent cation dependence and characterization of the divalent cation binding site of the fosfomycin resistance protein (FosA)."
      Bernat B.A., Laughlin L.T., Armstrong R.N.
      Biochemistry 38:7462-7469(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: METAL-BINDING SITES, MUTAGENESIS OF HIS-7; HIS-67 AND GLU-113.

    Entry informationi

    Entry nameiFOSA_SERMA
    AccessioniPrimary (citable) accession number: Q56415
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 59 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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3