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Q98GG1

- FOSX_RHILO

UniProt

Q98GG1 - FOSX_RHILO

Protein

Fosfomycin resistance protein FosX

Gene

fosX

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes the hydration of fosfomycin.1 Publication

    Cofactori

    Manganese.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi7 – 71Manganese
    Active sitei44 – 441Proton acceptorCurated
    Metal bindingi69 – 691Manganese
    Metal bindingi118 – 1181Manganese

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. response to antibiotic Source: UniProtKB-KW

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMLOT266835:GJ9L-2596-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fosfomycin resistance protein FosX
    Gene namesi
    Name:fosX
    Ordered Locus Names:mlr3345
    OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
    Taxonomic identifieri266835 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
    ProteomesiUP000000552: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441E → G: Decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 139139Fosfomycin resistance protein FosXPRO_0000164047Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi266835.mlr3345.

    Structurei

    Secondary structure

    1
    139
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 1312
    Helixi15 – 2612
    Beta strandi29 – 335
    Helixi34 – 363
    Beta strandi44 – 496
    Beta strandi52 – 587
    Beta strandi69 – 735
    Helixi76 – 783
    Helixi79 – 8911
    Beta strandi106 – 1105
    Beta strandi116 – 1205
    Helixi124 – 1296

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R9CX-ray1.83A/B1-139[»]
    ProteinModelPortaliQ98GG1.
    SMRiQ98GG1. Positions 1-130.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ98GG1.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0346.
    HOGENOMiHOG000232023.
    OMAiFDAREVY.
    OrthoDBiEOG6VXFB2.

    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.

    Q98GG1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIEGLSHMTF IVRDLERMTR ILEGVFDARE VYASDTEQFS LSREKFFLIG    50
    DIWVAIMQGE KLAERSYNHI AFKIDDADFD RYAERVGKLG LDMRPPRPRV 100
    EGEGRSIYFY DDDNHMFELH TGTLTERLAR KAKGLEAAQ 139
    Length:139
    Mass (Da):16,181
    Last modified:October 1, 2001 - v1
    Checksum:i8F9138A570B900F2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000012 Genomic DNA. Translation: BAB50255.1.
    RefSeqiNP_104469.1. NC_002678.2.

    Genome annotation databases

    EnsemblBacteriaiBAB50255; BAB50255; BAB50255.
    GeneIDi1227130.
    KEGGimlo:mlr3345.
    PATRICi22479521. VBIMesLot2464_2664.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000012 Genomic DNA. Translation: BAB50255.1 .
    RefSeqi NP_104469.1. NC_002678.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R9C X-ray 1.83 A/B 1-139 [» ]
    ProteinModelPortali Q98GG1.
    SMRi Q98GG1. Positions 1-130.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266835.mlr3345.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB50255 ; BAB50255 ; BAB50255 .
    GeneIDi 1227130.
    KEGGi mlo:mlr3345.
    PATRICi 22479521. VBIMesLot2464_2664.

    Phylogenomic databases

    eggNOGi COG0346.
    HOGENOMi HOG000232023.
    OMAi FDAREVY.
    OrthoDBi EOG6VXFB2.

    Enzyme and pathway databases

    BioCyci MLOT266835:GJ9L-2596-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q98GG1.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MAFF303099.
    2. "Mechanistic diversity of fosfomycin resistance in pathogenic microorganisms."
      Fillgrove K.L., Pakhomova S., Newcomer M.E., Armstrong R.N.
      J. Am. Chem. Soc. 125:15730-15731(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), FUNCTION, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-44.
      Strain: MAFF303099.

    Entry informationi

    Entry nameiFOSX_RHILO
    AccessioniPrimary (citable) accession number: Q98GG1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: October 1, 2001
    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, Complete proteome, Reference proteome

    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