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Q56415 (FOSA_SERMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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:
Glutathione transferase FosA

EC=2.5.1.18
Alternative name(s):
Fosfomycin resistance protein
Gene names
Name:fosA
Synonyms:fos
OrganismSerratia marcescens
Taxonomic identifier615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length141 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin. Ref.2

Catalytic activity

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

Cofactor

Manganese. Ref.2

Enzyme regulation

Requires the monovalent cation K+ for optimal activity.

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm Ref.1.

Sequence similarities

Belongs to the fosfomycin resistance protein family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 141141Glutathione transferase FosA
PRO_0000164044

Sites

Metal binding71Manganese
Metal binding671Manganese
Metal binding1131Manganese

Experimental info

Mutagenesis71H → A: Strong decrease in fosfomycin resistance. Ref.3
Mutagenesis71H → Q: Decrease in fosfomycin resistance. Ref.3
Mutagenesis671H → A: Loss of fosfomycin resistance. Ref.3
Mutagenesis671H → Q: Decrease in fosfomycin resistance. Ref.3
Mutagenesis1131E → A: Strong decrease in fosfomycin resistance. Ref.3
Mutagenesis1131E → Q: Decrease in fosfomycin resistance. Ref.3

Secondary structure

............................ 141
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q56415 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7BA4E5BF33FF3315

FASTA14115,959
        10         20         30         40         50         60 
MLQSLNHLTL AVSDLQKSVT FWHELLGLTL HARWNTGAYL TCGDLWVCLS YDEARQYVPP 

        70         80         90        100        110        120 
QESDYTHYAF TVAEEDFEPL SQRLEQAGVT IWKQNKSEGA SFYFLDPDGH KLELHVGSLA 

       130        140 
ARLAACREKP YAGMVFTSDE A 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M85195 Genomic DNA. Translation: AAA98399.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NPBX-ray2.50A/B/C/D/E/F1-141[»]
ProteinModelPortalQ56415.
SMRQ56415. Positions 1-140.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ56415.

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

EvolutionaryTraceQ56415.

Entry information

Entry nameFOSA_SERMA
AccessionPrimary (citable) accession number: Q56415
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: July 9, 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