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P15214 (GST_PROMI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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 S-transferase GST-6.0

EC=2.5.1.18
Alternative name(s):
GST B1-1
Gene names
Name:gstB
OrganismProteus mirabilis
Taxonomic identifier584 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length203 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. Beta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Direct protein sequencing
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 – 203203Glutathione S-transferase GST-6.0
PRO_0000185974

Regions

Domain1 – 8181GST N-terminal
Domain87 – 203117GST C-terminal
Region51 – 522Glutathione binding
Region65 – 662Glutathione binding
Region106 – 1072Glutathione binding

Sites

Binding site101Glutathione
Binding site351Glutathione

Experimental info

Sequence conflict201E → Q AA sequence Ref.3
Sequence conflict34 – 363TKK → RLL AA sequence Ref.3
Sequence conflict381Missing AA sequence Ref.4

Secondary structure

....................................... 203
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15214 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 2021F194D5CF105E

FASTA20322,852
        10         20         30         40         50         60 
MKLYYTPGSC SLSPHIVLRE TGLDFSIERI DLRTKKTESG KDFLAINPKG QVPVLQLDNG 

        70         80         90        100        110        120 
DILTEGVAIV QYLADLKPDR NLIAPPKALE RYHQIEWLNF LASEVHKGYS PLFSSDTPES 

       130        140        150        160        170        180 
YLPVVKNKLK SKFVYINDVL SKQKCVCGDH FTVADAYLFT LSQWAPHVAL DLTDLSHLQD 

       190        200 
YLARIAQRPN VHSALVTEGL IKE 

« Hide

References

[1]"Molecular cloning and overexpression of a glutathione transferase gene from Proteus mirabilis."
Perito B., Allocati N., Casalone E., Masulli M., Dragani B., Polsinelli M., Aceto A., Di Ilio C.
Biochem. J. 318:157-162(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AF 2924.
[2]"The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes."
Mignogna G., Allocati N., Aceto A., Piccolomini R., Di Ilio C., Barra D., Martini F.
Eur. J. Biochem. 211:421-425(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: AF 2924.
[3]"N-terminal region of Proteus mirabilis glutathione transferase is not homologous to mammalian and plant glutathione transferases."
Di Ilio C., Aceto A., Piccolomini R., Allocati N., Caccuri A.M., Barra D., Feferici G.
FEBS Lett. 250:57-59(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-38.
Strain: AF 2924.
[4]"Purification and characterization of a heterodimeric 23/20-kDa proteolytic fragment of bacterial glutathione transferase B1-1."
Aceto A., Dragani B., Allocati N., Masulli M., Petruzzelli R., Di Ilio C.
Arch. Biochem. Biophys. 328:302-308(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-5 AND 36-42.
[5]"A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications."
Rossjohn J., Polekhina G., Feil S.C., Allocati N., Masulli M., Di Ilio C., Parker M.W.
Structure 6:721-734(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38482 Genomic DNA. Translation: AAC44362.1.
PIRS71882.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PMTX-ray2.50A1-203[»]
2PMTX-ray2.70A/B/C/D1-203[»]
ProteinModelPortalP15214.
SMRP15214. Positions 1-201.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 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...

Other

EvolutionaryTraceP15214.

Entry information

Entry nameGST_PROMI
AccessionPrimary (citable) accession number: P15214
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 83 of the entry and version 2 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