Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q98GG1 (FOSX_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fosfomycin resistance protein FosX
Gene names
Name:fosX
Ordered Locus Names:mlr3345
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydration of fosfomycin. Ref.2

Cofactor

Manganese. Ref.2

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the fosfomycin resistance protein family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processresponse to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 139139Fosfomycin resistance protein FosX
PRO_0000164047

Sites

Active site441Proton acceptor Probable
Metal binding71Manganese
Metal binding691Manganese
Metal binding1181Manganese

Experimental info

Mutagenesis441E → G: Decrease in activity. Ref.2

Secondary structure

....................... 139
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q98GG1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 8F9138A570B900F2

FASTA13916,181
        10         20         30         40         50         60 
MIEGLSHMTF IVRDLERMTR ILEGVFDARE VYASDTEQFS LSREKFFLIG DIWVAIMQGE 

        70         80         90        100        110        120 
KLAERSYNHI AFKIDDADFD RYAERVGKLG LDMRPPRPRV EGEGRSIYFY DDDNHMFELH 

       130 
TGTLTERLAR KAKGLEAAQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB50255.1.
RefSeqNP_104469.1. NC_002678.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R9CX-ray1.83A/B1-139[»]
ProteinModelPortalQ98GG1.
SMRQ98GG1. Positions 1-130.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mlr3345.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB50255; BAB50255; BAB50255.
GeneID1227130.
KEGGmlo:mlr3345.
PATRIC22479521. VBIMesLot2464_2664.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0346.
HOGENOMHOG000232023.
OMAFDAREVY.
OrthoDBEOG6VXFB2.

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-2596-MONOMER.

Family and domain databases

Gene3D3.10.180.10. 1 hit.
InterProIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]
PfamPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMSSF54593. SSF54593. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ98GG1.

Entry information

Entry nameFOSX_RHILO
AccessionPrimary (citable) accession number: Q98GG1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2001
Last modified: June 11, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references