Reviewed, UniProtKB/Swiss-Prot P46436 (GST1_ASCSU)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase 1
    EC=2.5.1.18
Alternative name(s):
    GST class-sigma

Gene names

Name:

GST1

Organism

Ascaris suum (Pig roundworm) (Ascaris lumbricoides)

Taxonomic identifier

6253 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Ascaridida › Ascaridoidea › Ascarididae › Ascaris

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can also function as a GSH peroxidase.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Sequence similarities	Belongs to the GST superfamily. Sigma family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Molecular function	Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	glutathione transferase activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 206	205	Glutathione S-transferase 1		PRO_0000185922
Regions
	Domain	2 – 79	78	GST N-terminal
	Domain	81 – 206	126	GST C-terminal

Sequences

	Sequence		Length	Mass (Da)
	P46436-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B8366238A63DF399	FASTA	206	23,585
	10 20 30 40 50 60 MPQYKLTYFD IRGLGEGARL IFHQAGVKFE DNRLKREDWP ALKPKTPFGQ LPLLEVDGEV 70 80 90 100 110 120 LAQSAAIYRY LGRQFGLAGK TPMEEAQVDS IFDQFKDFMA ELRPCFRVLA GFEEGDKEKV 130 140 150 160 170 180 LKEVAVPARD KHLPLLEKFL AKSGSEYMVG KSVTWADLVI TDSLASWESL IPDFLSGHLQ 190 200 LKKYIEHVRE LPNIKKWIAE RPKTPY

References

[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: 8183318] [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: 9182731] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75502 mRNA. Translation: CAA53218.1. Y10613 Genomic DNA. Translation: CAA71620.1.
PIR	S38626.
3D structure databases
SMR	P46436. Positions 1-206.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.5.1.18. 649.
Family and domain databases
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012336. Thioredoxin-like_fold. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view]
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GST1_ASCSU

Accession

Primary (citable) accession number: P46436

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 40 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)