Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9I4K6 (FOSA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. 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
Ordered Locus Names:PA1129
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length135 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 By similarity.

Subcellular location

Cytoplasm By similarity.

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
Complete proteome
Reference proteome
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 – 135135Glutathione transferase FosA
PRO_0000164043

Sites

Metal binding71Manganese
Metal binding641Manganese
Metal binding1101Manganese

Secondary structure

............................ 135
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9I4K6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 0D75F174291A2366

FASTA13515,124
        10         20         30         40         50         60 
MLTGLNHLTL AVADLPASIA FYRDLLGFRL EARWDQGAYL ELGSLWLCLS REPQYGGPAA 

        70         80         90        100        110        120 
DYTHYAFGIA AADFARFAAQ LRAHGVREWK QNRSEGDSFY FLDPDGHRLE AHVGDLRSRL 

       130 
AACRQAPYAG MRFAD 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
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(2002) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG04518.1.
PIRE83503.
RefSeqNP_249820.1. NC_002516.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9I4K6.
SMRQ9I4K6. Positions 1-134.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA1129.

Protocols and materials databases

DNASU877785.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG04518; AAG04518; PA1129.
GeneID877785.
KEGGpae:PA1129.
PATRIC19836576. VBIPseAer58763_1174.

Organism-specific databases

PseudoCAPPA1129.

Phylogenomic databases

eggNOGCOG0346.
HOGENOMHOG000232023.
OMAHYAFSIA.
OrthoDBEOG6VXFB2.
PhylomeDBQ9I4K6.

Family and domain databases

Gene3D3.10.180.10. 1 hit.
InterProIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR025870. Glyoxalase-like_dom.
[Graphical view]
PfamPF12681. Glyoxalase_2. 1 hit.
[Graphical view]
SUPFAMSSF54593. SSF54593. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9I4K6.

Entry information

Entry nameFOSA_PSEAE
AccessionPrimary (citable) accession number: Q9I4K6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 77 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