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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...

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: October 14, 2015
This is version 64 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

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 one 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.