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Protein

Glutathione transferase FosA

Gene

fosA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi64 – 641Manganese
Metal bindingi110 – 1101Manganese

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione transferase FosA (EC:2.5.1.18)
Alternative name(s):
Fosfomycin resistance protein
Gene namesi
Name:fosA
Ordered Locus Names:PA1129
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA1129.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 135135Glutathione transferase FosAPRO_0000164043Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi208964.PA1129.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1312Combined sources
Helixi15 – 2410Combined sources
Beta strandi29 – 346Combined sources
Beta strandi37 – 426Combined sources
Beta strandi45 – 517Combined sources
Beta strandi60 – 623Combined sources
Beta strandi64 – 696Combined sources
Helixi71 – 733Combined sources
Helixi74 – 8310Combined sources
Beta strandi88 – 903Combined sources
Beta strandi94 – 963Combined sources
Beta strandi98 – 1025Combined sources
Beta strandi108 – 1136Combined sources
Helixi116 – 12510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LQKX-ray1.35A/B1-135[»]
1LQOX-ray2.00A/B1-135[»]
1LQPX-ray1.19A/B1-135[»]
1NKIX-ray0.95A/B1-135[»]
1NNRX-ray2.25A/B1-135[»]
ProteinModelPortaliQ9I4K6.
SMRiQ9I4K6. Positions 1-134.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I4K6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0346.
HOGENOMiHOG000232023.
InParanoidiQ9I4K6.
OMAiGAYLTCG.
OrthoDBiEOG6VXFB2.
PhylomeDBiQ9I4K6.

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR025870. Glyoxalase-like_dom.
[Graphical view]
PfamiPF12681. Glyoxalase_2. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9I4K6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTGLNHLTL AVADLPASIA FYRDLLGFRL EARWDQGAYL ELGSLWLCLS
60 70 80 90 100
REPQYGGPAA DYTHYAFGIA AADFARFAAQ LRAHGVREWK QNRSEGDSFY
110 120 130
FLDPDGHRLE AHVGDLRSRL AACRQAPYAG MRFAD
Length:135
Mass (Da):15,124
Last modified:March 1, 2001 - v1
Checksum:i0D75F174291A2366
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG04518.1.
PIRiE83503.
RefSeqiNP_249820.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG04518; AAG04518; PA1129.
GeneIDi877785.
KEGGipae:PA1129.
PATRICi19836576. VBIPseAer58763_1174.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG04518.1.
PIRiE83503.
RefSeqiNP_249820.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LQKX-ray1.35A/B1-135[»]
1LQOX-ray2.00A/B1-135[»]
1LQPX-ray1.19A/B1-135[»]
1NKIX-ray0.95A/B1-135[»]
1NNRX-ray2.25A/B1-135[»]
ProteinModelPortaliQ9I4K6.
SMRiQ9I4K6. Positions 1-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA1129.

Protocols and materials databases

DNASUi877785.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG04518; AAG04518; PA1129.
GeneIDi877785.
KEGGipae:PA1129.
PATRICi19836576. VBIPseAer58763_1174.

Organism-specific databases

PseudoCAPiPA1129.

Phylogenomic databases

eggNOGiCOG0346.
HOGENOMiHOG000232023.
InParanoidiQ9I4K6.
OMAiGAYLTCG.
OrthoDBiEOG6VXFB2.
PhylomeDBiQ9I4K6.

Miscellaneous databases

EvolutionaryTraceiQ9I4K6.

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR025870. Glyoxalase-like_dom.
[Graphical view]
PfamiPF12681. Glyoxalase_2. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. "Crystal structure of a genomically encoded fosfomycin resistance protein (FosA) at 1.19 A resolution by MAD phasing off the L-III edge of Tl(+)."
    Rife C.L., Pharris R.E., Newcomer M.E., Armstrong R.N.
    J. Am. Chem. Soc. 124:11001-11003(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) IN COMPLEX WITH FOSFOMYCIN, FUNCTION, COFACTOR.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiFOSA_PSEAE
AccessioniPrimary (citable) accession number: Q9I4K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 81 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, Complete proteome, Reference proteome

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.