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Protein

Glutathione transferase FosA

Gene

fosA

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

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

Mn2+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

GO - Biological processi

Complete GO annotation...

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

GO - Cellular componenti

Complete GO annotation...

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 – 1310Combined sources
Helixi15 – 239Combined sources
Beta strandi29 – 346Combined sources
Beta strandi37 – 426Combined sources
Beta strandi45 – 517Combined sources
Helixi60 – 623Combined sources
Beta strandi67 – 715Combined sources
Turni74 – 763Combined sources
Helixi77 – 8610Combined sources
Beta strandi91 – 933Combined sources
Beta strandi97 – 1059Combined sources
Beta strandi111 – 1166Combined sources
Helixi119 – 12810Combined sources
Beta strandi135 – 1373Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MLQSLNHLTL AVSDLQKSVT FWHELLGLTL HARWNTGAYL TCGDLWVCLS
60 70 80 90 100
YDEARQYVPP QESDYTHYAF TVAEEDFEPL SQRLEQAGVT IWKQNKSEGA
110 120 130 140
SFYFLDPDGH KLELHVGSLA ARLAACREKP YAGMVFTSDE A
Length:141
Mass (Da):15,959
Last modified:November 1, 1996 - v1
Checksum:i7BA4E5BF33FF3315
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85195 Genomic DNA. Translation: AAA98399.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85195 Genomic DNA. Translation: AAA98399.1.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ56415.

Miscellaneous databases

EvolutionaryTraceiQ56415.

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

  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: January 7, 2015
This is version 62 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

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.