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Protein

Glutathione S-transferase

Gene
N/A
Organism
Antechinus stuartii (Brown marsupial mouse)
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 sitei9 – 91GlutathioneBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione metabolic process Source: UniProtKB
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-alpha
Cleaved into the following chain:
OrganismiAntechinus stuartii (Brown marsupial mouse)
Taxonomic identifieri9283 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDasyuromorphiaDasyuridaeAntechinus

Subcellular locationi

Cytoplasm By similarity

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 – 221221Glutathione S-transferasePRO_0000185803Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 221220Glutathione S-transferase, N-terminally processedPRO_0000421784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP80894.
SMRiP80894. Positions 2-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8280GST N-terminalAdd
BLAST
Domaini84 – 208125GST C-terminalAdd
BLAST

Region

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

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG053749.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80894-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGEQNIKYF NIKGRMEAIR WLLAVAGVEF EEKFFETKEQ LQKLKETVLL
60 70 80 90 100
FQQVPMVEID GMKLVQTRAI LHYIAEKYNL LGKDMKEHAQ IIMYSEGTMD
110 120 130 140 150
LMELIMIYPF LKGEEKKQRL VEIANKAKGR YFPAFENVLK THGQNFLVGN
160 170 180 190 200
QLSMADVQLF EAILMVEEKV PDALSGFPLL QAFKTRISNI PTVKTFLAPG
210 220
SKRKPVPDAK YVEDIIKIFY F
Length:221
Mass (Da):25,534
Last modified:November 1, 1997 - v1
Checksum:i03B185BCC44B570F
GO

Cross-referencesi

3D structure databases

ProteinModelPortaliP80894.
SMRiP80894. Positions 2-219.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG053749.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of a marsupial glutathione transferase, a class Alpha enzyme from Brown Antechinus (Antechinus stuartii)."
    Bolton R.M., Curstedt L., Cederlund E., Hjelmqvist L., Mannervik B., Ahokas J.T., Joernvall H.
    FEBS Lett. 406:216-219(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiGSTA1_ANTST
AccessioniPrimary (citable) accession number: P80894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 66 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.