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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)DescriptionActionsGraphical viewLength
Binding sitei10Glutathione1 Publication1
Binding sitei35Glutathione1 Publication1
Binding sitei52Glutathione; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei99Glutathione1 Publication1

GO - Molecular functioni

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaeProteus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001859741 – 203Glutathione S-transferase GST-6.0Add BLAST203

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi529507.PMI1384.

Structurei

Secondary structure

1203
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi12 – 20Combined sources9
Beta strandi26 – 31Combined sources6
Turni32 – 35Combined sources4
Helixi43 – 45Combined sources3
Beta strandi54 – 56Combined sources3
Beta strandi62 – 65Combined sources4
Helixi66 – 74Combined sources9
Helixi78 – 80Combined sources3
Helixi89 – 103Combined sources15
Helixi106 – 109Combined sources4
Helixi110 – 113Combined sources4
Beta strandi115 – 117Combined sources3
Turni119 – 121Combined sources3
Helixi122 – 140Combined sources19
Beta strandi143 – 145Combined sources3
Beta strandi148 – 150Combined sources3
Helixi153 – 162Combined sources10
Helixi166 – 168Combined sources3
Helixi176 – 186Combined sources11
Helixi189 – 197Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP15214.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 81GST N-terminalAdd BLAST81
Domaini87 – 203GST C-terminalAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni65 – 66Glutathione binding1 Publication2
Regioni103 – 107Glutathione binding1 Publication5

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108K3A. Bacteria.
COG0625. LUCA.

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)DescriptionActionsGraphical viewLength
Sequence conflicti20E → Q AA sequence (PubMed:2661269).Curated1
Sequence conflicti34 – 36TKK → RLL AA sequence (PubMed:2661269).Curated3
Sequence conflicti38Missing AA sequence (PubMed:8645008).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38482 Genomic DNA. Translation: AAC44362.1.
PIRiS71882.
RefSeqiWP_004248152.1. NZ_LTBK01000024.1.

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_LTBK01000024.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi529507.PMI1384.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6801758.

Phylogenomic databases

eggNOGiENOG4108K3A. Bacteria.
COG0625. LUCA.

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...

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: November 2, 2016
This is version 99 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

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 one 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.