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Reviewed, UniProtKB/Swiss-Prot P45875 (GST_XANCP)

Last modified November 24, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier340 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglutathione transferase activity

Inferred from electronic annotation. Source: 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

Sites

Active site101 By similarity
Active site1021 By similarity

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
P45875-1 [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: 12024217] [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: 8342943] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-32.

Cross-references

Sequence databases

AE008922 Genomic DNA. Translation: AAM40239.1.
PIRS35583.
RefSeqNP_636315.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1001477.
GenomeReviewsGene locus XCC0929 in contig AE008922_GR.
KEGGxcc:XCC0929.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP45875.
OMAFSPLACS

Enzyme and pathway databases

BioCycXCAM190485:XCC0929-MON.
BRENDA2.5.1.18. 281360.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
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: November 24, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents