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Protein

Fosfomycin resistance protein FosX

Gene

fosX

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

Functioni

Catalyzes the hydration of fosfomycin.1 Publication

Cofactori

Mn2+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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 – 1312Combined sources
Helixi15 – 2612Combined sources
Beta strandi29 – 335Combined sources
Helixi34 – 363Combined sources
Beta strandi44 – 496Combined sources
Beta strandi52 – 587Combined sources
Beta strandi69 – 735Combined sources
Helixi76 – 783Combined sources
Helixi79 – 8911Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi116 – 1205Combined sources
Helixi124 – 1296Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiNHIAFRI.
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

        10         20         30         40         50
MIEGLSHMTF IVRDLERMTR ILEGVFDARE VYASDTEQFS LSREKFFLIG
60 70 80 90 100
DIWVAIMQGE KLAERSYNHI AFKIDDADFD RYAERVGKLG LDMRPPRPRV
110 120 130
EGEGRSIYFY DDDNHMFELH TGTLTERLAR KAKGLEAAQ
Length:139
Mass (Da):16,181
Last modified:October 1, 2001 - v1
Checksum:i8F9138A570B900F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB50255.1.
RefSeqiWP_010911601.1. NC_002678.2.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB50255.1.
RefSeqiWP_010911601.1. NC_002678.2.

3D structure databases

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

Protein-protein interaction databases

STRINGi266835.mlr3345.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0346.
HOGENOMiHOG000232023.
OMAiNHIAFRI.
OrthoDBiEOG6VXFB2.

Enzyme and pathway databases

BioCyciMLOT266835:GJ9L-2596-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ98GG1.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 68 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

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.