Q12390 (GST2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase 2
EC=2.5.1.18

Alternative name(s):
GST-II

Gene names

Name:	GTT2
Ordered Locus Names:	YLL060C
ORF Names:	L0560

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.6
Subunit structure	Homodimer. Ref.6
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from direct assay Ref.5. Source: SGD
Cellular_component	mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD
Molecular_function	glutathione transferase activity Inferred from direct assay Ref.5. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 233

233

Glutathione S-transferase 2

PRO_0000185988

Regions

Domain

17 – 101

85

GST N-terminal

Domain

106 – 233

128

GST C-terminal

Region

85 – 86

2

Glutathione binding

Sites

Binding site

29

1

Glutathione; via amide nitrogen

Binding site

58

1

Glutathione

Binding site

72

1

Glutathione; via amide nitrogen and carbonyl oxygen

Binding site

133

1

Glutathione

Experimental info

Mutagenesis

27

1

G → A: Reduced enzyme activity. Ref.6

Mutagenesis

27

1

G → C, F or S: Loss of enzyme activity. Ref.6

Mutagenesis

129

1

S → A: Reduced enzyme activity. Ref.6

Mutagenesis

133

1

H → A: Loss of enzyme activity. Ref.6

Secondary structure

1

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233

Helix Strand Turn

Details...

Beta strand

20 – 23

4

Helix

28 – 39

12

Helix

43 – 45

3

Beta strand

47 – 50

4

Helix

53 – 55

3

Helix

57 – 59

3

Helix

61 – 66

6

Beta strand

74 – 76

3

Beta strand

82 – 85

4

Helix

86 – 96

11

Beta strand

101 – 103

3

Helix

107 – 123

17

Helix

125 – 135

11

Turn

141 – 143

3

Helix

149 – 170

22

Beta strand

178 – 180

3

Helix

183 – 197

15

Helix

207 – 218

12

Helix

220 – 225

6

Sequences

	Sequence		Length	Mass (Da)
	Q12390 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B5EE0E47D5A37175	FASTA	233	26,340
	10 20 30 40 50 60 MNGRGFLIYN GGEKMKQKMI IYDTPAGPYP ARVRIALAEK NMLSSVQFVR INLWKGEHKK 70 80 90 100 110 120 PEFLAKNYSG TVPVLELDDG TLIAECTAIT EYIDALDGTP TLTGKTPLEK GVIHMMNKRA 130 140 150 160 170 180 ELELLDPVSV YFHHATPGLG PEVELYQNKE WGLRQRDKAL HGMHYFDTVL RERPYVAGDS 190 200 210 220 230 FSMADITVIA GLIFAAIVKL QVPEECEALR AWYKRMQQRP SVKKLLEIRS KSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces cerevisiae including the subtelomeric region of the left arm." Wedler H., Wambutt R. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"A novel membrane-bound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae." Choi J.H., Lou W., Vancura A. J. Biol. Chem. 273:29915-29922(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family." Ma X.X., Jiang Y.L., He Y.X., Bao R., Chen Y., Zhou C.Z. EMBO Rep. 10:1320-1326(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-27; SER-129 AND HIS-133, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z47973 Genomic DNA. Translation: CAA87997.1.
Z73165 Genomic DNA. Translation: CAA97513.1.
AY557940 Genomic DNA. Translation: AAS56266.1.
BK006945 Genomic DNA. Translation: DAA09265.1.

PIR

S50960.

RefSeq

NP_013040.1. NM_001181880.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ERF	X-ray	2.23	A	1-233	[»]
3ERG	X-ray	2.20	A/B	1-233	[»]
3IBH	X-ray	2.10	A	1-233	[»]

ProteinModelPortal

Q12390.

SMR

Q12390. Positions 19-226.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2981N.

IntAct

Q12390. 1 interaction.

MINT

MINT-2785201.

STRING

4932.YLL060C.

Proteomic databases

PaxDb

Q12390.

PeptideAtlas

Q12390.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLL060C; YLL060C; YLL060C.

GeneID

850666.

KEGG

sce:YLL060C.

Organism-specific databases

CYGD

YLL060c.

SGD

S000003983. GTT2.

Phylogenomic databases

eggNOG

COG0625.

HOGENOM

HOG000125751.

OMA

KGVIHMM.

OrthoDB

EOG4BCHXH.

Enzyme and pathway databases

SABIO-RK

Q12390.

Gene expression databases

Genevestigator

Q12390.

GermOnline

YLL060C. Saccharomyces cerevisiae.

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.
[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...

Other

EvolutionaryTrace

Q12390.

NextBio

966644.

Entry information

Entry name

GST2_YEAST

Accession

Primary (citable) accession number: Q12390
Secondary accession number(s): D6VXU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program