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Protein

Glutathione S-transferase

Gene
N/A
Organism
Musca domestica (House fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 sitei46 – 461GlutathioneBy similarity
Binding sitei77 – 771GlutathioneBy similarity
Binding sitei81 – 811GlutathioneBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase (EC:2.5.1.18)
Alternative name(s):
GST class-sigma
OrganismiMusca domestica (House fly)
Taxonomic identifieri7370 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaMuscoideaMuscidaeMusca

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Glutathione S-transferasePRO_0000185919Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP46437.
SMRiP46437. Positions 39-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 11778GST N-terminalAdd
BLAST
Domaini119 – 241123GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 892Glutathione bindingBy similarity
Regioni101 – 1022Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Sigma 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.

P46437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEAPAAPP AEGEAPAAPA EGEAPPPAEG EAPPAEPVKN TYTLFYFNVK
60 70 80 90 100
ALAEPLRYLF AYGGIEYEDV RVTRDEWPAL KPTMPMGQMP VLEVNGKRVH
110 120 130 140 150
QSISMARFLA KTVGLCGATP WEDLQVDIVV DTINDFRLKI AVVSYEPEDE
160 170 180 190 200
IKEKKLVTLN NEVIPFYLEK LEQTVKDNDG HLALNKLTWA DVYFAGILDY
210 220 230 240
MNYMVKRDIL EQYPALRGVV DSVNALEPIK AWIEKRPQTE V
Length:241
Mass (Da):26,964
Last modified:November 1, 1995 - v1
Checksum:i6A8FBD67ADDDEDFA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02616 mRNA. Translation: AAA03434.1.
RefSeqiNP_001273827.1. NM_001286898.1.

Genome annotation databases

GeneIDi101890455.
KEGGimde:101890455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02616 mRNA. Translation: AAA03434.1.
RefSeqiNP_001273827.1. NM_001286898.1.

3D structure databases

ProteinModelPortaliP46437.
SMRiP46437. Positions 39-241.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101890455.
KEGGimde:101890455.

Organism-specific databases

CTDi101890455.

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. Franciosa H.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Cooper.
    Tissue: Head.

Entry informationi

Entry nameiGST_MUSDO
AccessioniPrimary (citable) accession number: P46437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 4, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. 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.