Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione S-transferase GST-6.0

Gene

gstB

Organism
Proteus mirabilis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Glutathione1 Publication
Binding sitei35 – 351Glutathione1 Publication

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase GST-6.0 (EC:2.5.1.18)
Alternative name(s):
GST B1-1
Gene namesi
Name:gstB
OrganismiProteus mirabilis
Taxonomic identifieri584 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Subcellular locationi

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 – 203203Glutathione S-transferase GST-6.0PRO_0000185974Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi12 – 209Combined sources
Beta strandi26 – 316Combined sources
Turni32 – 354Combined sources
Helixi43 – 453Combined sources
Beta strandi54 – 563Combined sources
Beta strandi62 – 654Combined sources
Helixi66 – 749Combined sources
Helixi78 – 803Combined sources
Helixi89 – 10315Combined sources
Helixi106 – 1094Combined sources
Helixi110 – 1134Combined sources
Beta strandi115 – 1173Combined sources
Turni119 – 1213Combined sources
Helixi122 – 14019Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi148 – 1503Combined sources
Helixi153 – 16210Combined sources
Helixi166 – 1683Combined sources
Helixi176 – 18611Combined sources
Helixi189 – 1979Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PMTX-ray2.50A1-203[»]
2PMTX-ray2.70A/B/C/D1-203[»]
ProteinModelPortaliP15214.
SMRiP15214. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15214.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8181GST N-terminalAdd
BLAST
Domaini87 – 203117GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 522Glutathione binding
Regioni65 – 662Glutathione binding
Regioni106 – 1072Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Beta family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLYYTPGSC SLSPHIVLRE TGLDFSIERI DLRTKKTESG KDFLAINPKG
60 70 80 90 100
QVPVLQLDNG DILTEGVAIV QYLADLKPDR NLIAPPKALE RYHQIEWLNF
110 120 130 140 150
LASEVHKGYS PLFSSDTPES YLPVVKNKLK SKFVYINDVL SKQKCVCGDH
160 170 180 190 200
FTVADAYLFT LSQWAPHVAL DLTDLSHLQD YLARIAQRPN VHSALVTEGL

IKE
Length:203
Mass (Da):22,852
Last modified:April 1, 1993 - v2
Checksum:i2021F194D5CF105E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201E → Q AA sequence (PubMed:2661269).Curated
Sequence conflicti34 – 363TKK → RLL AA sequence (PubMed:2661269).Curated
Sequence conflicti38 – 381Missing AA sequence (PubMed:8645008).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38482 Genomic DNA. Translation: AAC44362.1.
PIRiS71882.
RefSeqiWP_004248152.1. NZ_KN150749.1.

Genome annotation databases

GeneIDi6801758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38482 Genomic DNA. Translation: AAC44362.1.
PIRiS71882.
RefSeqiWP_004248152.1. NZ_KN150749.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PMTX-ray2.50A1-203[»]
2PMTX-ray2.70A/B/C/D1-203[»]
ProteinModelPortaliP15214.
SMRiP15214. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6801758.

Miscellaneous databases

EvolutionaryTraceiP15214.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1995) [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(1992) [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(1988) [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(1995) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.

Entry informationi

Entry nameiGST_PROMI
AccessioniPrimary (citable) accession number: P15214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1993
Last modified: April 1, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.