P30102 (GSTY2_ISSOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase Y-2
EC=2.5.1.18

Gene names

Name:

GSTY2

Organism

Issatchenkia orientalis (Yeast) (Candida krusei)

Taxonomic identifier

4909 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Pichiaceae › Pichia

Protein attributes

Sequence length	191 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.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Induction	By O-dinitrobenzene.
Sequence similarities	Belongs to the GST superfamily. 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 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 191	190	Glutathione S-transferase Y-2		PRO_0000185983
Regions
	Domain	2 – 80	79	GST N-terminal
	Domain	85 – 191	107	GST C-terminal

Sequences

	Sequence		Length	Mass (Da)
	P30102 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 3BD1849C2C91363D	FASTA	191	21,652
	10 20 30 40 50 60 MTFATVYIKP HTPRGDWLAS LGQYVGLEIK TVDYKSAEAS KFEELFPLKR VPALVTPNGF 70 80 90 100 110 120 QLTELIAIVE YIVAKGSKPE LSGKTTEERA TNTRWLSFFN SDFVQAAGGY FMGPNDEIKQ 130 140 150 160 170 180 QSLQTMLSLL EYIDKHLSQS KYFTNNTILT ADIFAFQIFA MAKQFGVDFT HYPNVERFTG 190 EVSQHPIIKN M

References

[1]	"Nucleotide sequence of the yeast glutathione S-transferase cDNA." Tamaki H., Kumagai H., Tochikura T. Biochim. Biophys. Acta 1089:276-279(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Glutathione S-transferase in yeast: induction of mRNA, cDNA cloning and expression in Escherichia coli." Tamaki H., Kumagai H., Tochikura T. Biochem. Biophys. Res. Commun. 172:669-675(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16 AND 164-189.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57957 mRNA. Translation: CAA41025.1.
PIR	S16178.
3D structure databases
ProteinModelPortal	P30102.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 1 hit.
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. [Graphical view]
Pfam	PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view]
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSTY2_ISSOR

Accession

Primary (citable) accession number: P30102

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program