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Protein

Glutathione S-transferase P 1

Gene
N/A
Organism
Bufo bufo (European toad)
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 sitei7 – 71GlutathioneBy similarity
Binding sitei13 – 131GlutathioneBy similarity
Binding sitei38 – 381GlutathioneBy similarity
Binding sitei44 – 441GlutathioneBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase P 1 (EC:2.5.1.18)
Alternative name(s):
BBGSTP1-1
GST class-pi
OrganismiBufo bufo (European toad)
Taxonomic identifieri8384 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaBufonidaeBufo

Subcellular locationi

  • Cytoplasm By similarity
  • Mitochondrion By similarity
  • Nucleus By similarity

  • Note: The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Glutathione S-transferase P 1PRO_0000185908Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP81942.
SMRiP81942. Positions 1-209.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8080GST N-terminalAdd
BLAST
Domaini82 – 203122GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 522Glutathione bindingBy similarity
Regioni64 – 652Glutathione bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG108324.

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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81942-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PEYTIIYFNA RGRCEAMRML MADQGAQWKE EVVTSDDWQK GDLKKAAVYG
60 70 80 90 100
QLPGFKDGDF TLYQSNAMLR LLARNHDLYG KNPREASLID MVNDGVEDLR
110 120 130 140 150
LKYLKMIYQN YENGKDDYVK ALPTNLGHFE RLLASNNEGK GFVVGAHISF
160 170 180 190 200
ADYNLVDLLH NHLVLAPDCL SGFPLLCAYV KRISSRPKLE AYLSSDAHKK
210
RPINGNGKQQ
Length:210
Mass (Da):23,820
Last modified:May 1, 2000 - v1
Checksum:iAC835C0390F3A71D
GO

Cross-referencesi

3D structure databases

ProteinModelPortaliP81942.
SMRiP81942. Positions 1-209.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG108324.

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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Amphibian embryo glutathione transferase: amino acid sequence and structural properties."
    Sacchetta P., Petruzzelli R., Melino S., Bucciarelli T., Pennelli A., Amicarelli F., Miranda M., Di Ilio C.
    Biochem. J. 322:679-680(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Embryo.

Entry informationi

Entry nameiGSTP1_BUFBU
AccessioniPrimary (citable) accession number: P81942
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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.