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Protein

Glutathione S-transferase

Gene
N/A
Organism
Hyoscyamus muticus (Egyptian henbane)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei11 – 111GlutathioneBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Auxin signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase (EC:2.5.1.18)
Alternative name(s):
25 kDa auxin-binding protein
GST class-phi
OrganismiHyoscyamus muticus (Egyptian henbane)
Taxonomic identifieri35626 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeHyoscyameaeHyoscyamus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Glutathione S-transferasePRO_0000185854Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP46423.
SMRiP46423. Positions 2-206.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8282GST N-terminalAdd
BLAST
Domaini89 – 212124GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 412Glutathione bindingBy similarity
Regioni53 – 542Glutathione bindingBy similarity
Regioni66 – 672Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Phi 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.

P46423-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGMKLHGPAM SPAVMRVIAT LKEKDLDFEL VPVNMQAGDH KKEPFITLNP
60 70 80 90 100
FGQVPAFEDG DLKLFESRAI TQYIAHTYAD KGNQLLANDP KKMAIMSVWM
110 120 130 140 150
EVESQKFDPV ASKLTFEIVI KPMLGMVTDD AAVAENEEKL GKVLDVYESR
160 170 180 190 200
LKDSKYLGGD SFTLADLHHA PAMNYLMGTK VKSLFDSRPH VSAWCADILA
210
RPAWSKAIEY KQ
Length:212
Mass (Da):23,677
Last modified:November 1, 1995 - v1
Checksum:i9FFDB1A6A4582AD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78203 mRNA. Translation: CAA55039.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78203 mRNA. Translation: CAA55039.1.

3D structure databases

ProteinModelPortaliP46423.
SMRiP46423. Positions 2-206.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. "A soluble auxin-binding protein from Hyoscyamus muticus is a glutathione S-transferase."
    Bilang J., Macdonald H., King P.J., Sturm A.
    Plant Physiol. 102:29-34(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiGSTF_HYOMU
AccessioniPrimary (citable) accession number: P46423
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.