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Q56415

- FOSA_SERMA

UniProt

Q56415 - FOSA_SERMA

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Protein

Glutathione transferase FosA

Gene

fosA

Organism
Serratia marcescens
Status
Reviewed - 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

Manganese.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

  1. glutathione transferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. response to antibiotic Source: UniProtKB-KW
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

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
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 – 1310
Helixi15 – 239
Beta strandi29 – 346
Beta strandi37 – 426
Beta strandi45 – 517
Helixi60 – 623
Beta strandi67 – 715
Turni74 – 763
Helixi77 – 8610
Beta strandi91 – 933
Beta strandi97 – 1059
Beta strandi111 – 1166
Helixi119 – 12810
Beta strandi135 – 1373

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
Links Updated
M85195 Genomic DNA. Translation: AAA98399.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M85195 Genomic DNA. Translation: AAA98399.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NPB X-ray 2.50 A/B/C/D/E/F 1-141 [» ]
ProteinModelPortali Q56415.
SMRi Q56415. Positions 1-140.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK Q56415.

Miscellaneous databases

EvolutionaryTracei Q56415.

Family and domain databases

Gene3Di 3.10.180.10. 1 hit.
InterProi IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view ]
Pfami PF00903. Glyoxalase. 1 hit.
[Graphical view ]
SUPFAMi SSF54593. SSF54593. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 60 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