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P46436

- GST1_ASCSU

UniProt

P46436 - GST1_ASCSU

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Protein
Glutathione S-transferase 1
Gene
GST1
Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Status
Reviewed - 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. Can also function as a GSH peroxidase.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Glutathione By similarity
Binding sitei39 – 391Glutathione By similarity
Binding sitei43 – 431Glutathione By similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 1 (EC:2.5.1.18)
Alternative name(s):
GST class-sigma
Gene namesi
Name:GST1
OrganismiAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifieri6253 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 206205Glutathione S-transferase 1
PRO_0000185922Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP46436.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7978GST N-terminal
Add
BLAST
Domaini81 – 206126GST C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 512Glutathione binding By similarity
Regioni63 – 642Glutathione binding By similarity

Sequence similaritiesi

Belongs to the GST superfamily. Sigma family.

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.

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

P46436-1 [UniParc]FASTAAdd to Basket

« Hide

MPQYKLTYFD IRGLGEGARL IFHQAGVKFE DNRLKREDWP ALKPKTPFGQ    50
LPLLEVDGEV LAQSAAIYRY LGRQFGLAGK TPMEEAQVDS IFDQFKDFMA 100
ELRPCFRVLA GFEEGDKEKV LKEVAVPARD KHLPLLEKFL AKSGSEYMVG 150
KSVTWADLVI TDSLASWESL IPDFLSGHLQ LKKYIEHVRE LPNIKKWIAE 200
RPKTPY 206
Length:206
Mass (Da):23,585
Last modified:January 23, 2007 - v3
Checksum:iB8366238A63DF399
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75502 mRNA. Translation: CAA53218.1.
Y10613 Genomic DNA. Translation: CAA71620.1.
PIRiS38626.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75502 mRNA. Translation: CAA53218.1 .
Y10613 Genomic DNA. Translation: CAA71620.1 .
PIRi S38626.

3D structure databases

ProteinModelPortali P46436.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and expression of a cDNA encoding glutathione S-transferase from Ascaris suum."
    Liebau E., Schoenberger O.L., Walter R.D., Henkle-Duehrsen K.J.
    Mol. Biochem. Parasitol. 63:167-170(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-41.
  2. "Structural and functional analysis of a glutathione S-transferase from Ascaris suum."
    Liebau E., Eckelt V.H., Wildenburg G., Teesdale-Spittle P., Brophy P.M., Walter R.D., Henkle-Duehrsen K.
    Biochem. J. 324:659-666(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiGST1_ASCSU
AccessioniPrimary (citable) accession number: P46436
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 54 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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