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

P45875 (GST_XANCP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 S-transferase GST-4.5

EC=2.5.1.18
Gene names
Name:gst
Ordered Locus Names:XCC0929
OrganismXanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]
Taxonomic identifier190485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 204204Glutathione S-transferase GST-4.5
PRO_0000185976

Regions

Domain1 – 7777GST N-terminal
Domain83 – 204122GST C-terminal
Region61 – 622Glutathione binding By similarity

Sites

Binding site101Glutathione By similarity
Binding site491Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Binding site1021Glutathione By similarity

Experimental info

Sequence conflict221C → G AA sequence Ref.2
Sequence conflict261E → D AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P45875 [UniParc].

Last modified July 11, 2002. Version 3.
Checksum: F6302C321EB1F86F

FASTA20422,321
        10         20         30         40         50         60 
MKLYTKPGAC SLADHIVLRW SCLPFELTVV DAATMKSPDY LRLNPAGAVP LLVVDQWALT 

        70         80         90        100        110        120 
QNAAILNYIA DTAPLTGLGG DGTARSRAEI NRWIAFVNAD LHPTFKPLFG STAYLQEDAL 

       130        140        150        160        170        180 
IQRSHEDART KLRTLYTRVD AHLQGRNWLA GDTHTGADAY LFVTLRWAHK AGVDLSGLSA 

       190        200 
LDAFFQRMLA DADVQAALQA EGLN 

« Hide

References

« Hide 'large scale' references
[1]"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. expand/collapse author list , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33913 / NCPPB 528 / LMG 568.
[2]"Characterization of glutathione transferase from Xanthomonas campestris."
di Ilio C., Aceto A., Allocati N., Piccolomini R., Bucciarelli T., Dragani B., Faraone A., Sacchetta P., Petruzzelli R., Federici G.
Arch. Biochem. Biophys. 305:110-114(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008922 Genomic DNA. Translation: AAM40239.1.
PIRS35583.
RefSeqNP_636315.1. NC_003902.1.

3D structure databases

ProteinModelPortalP45875.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190485.XCC0929.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM40239; AAM40239; XCC0929.
GeneID1001477.
KEGGxcc:XCC0929.
PATRIC24072543. VBIXanCam115730_1001.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125748.
KOK00799.
OMAGRLAGPY.
OrthoDBEOG6H1Q01.
ProtClustDBCLSK881285.

Enzyme and pathway databases

BioCycXCAM190485:GIXZ-928-MONOMER.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGST_XANCP
AccessionPrimary (citable) accession number: P45875
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 11, 2002
Last modified: April 16, 2014
This is version 92 of the entry and version 3 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