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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 – 81GlutathioneBy similarity
Binding sitei39 – 391GlutathioneBy similarity
Binding sitei43 – 431GlutathioneBy 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 1PRO_0000185922Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP46436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 512Glutathione bindingBy similarity
Regioni63 – 642Glutathione 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.

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

P46436-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPQYKLTYFD IRGLGEGARL IFHQAGVKFE DNRLKREDWP ALKPKTPFGQ
60 70 80 90 100
LPLLEVDGEV LAQSAAIYRY LGRQFGLAGK TPMEEAQVDS IFDQFKDFMA
110 120 130 140 150
ELRPCFRVLA GFEEGDKEKV LKEVAVPARD KHLPLLEKFL AKSGSEYMVG
160 170 180 190 200
KSVTWADLVI TDSLASWESL IPDFLSGHLQ LKKYIEHVRE LPNIKKWIAE

RPKTPY
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: October 1, 2014
This is version 55 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