P41043 (GST1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase S1
EC=2.5.1.18

Alternative name(s):
GST class-sigma 1
Glutathione S-transferase 2

Gene names

Name:	GstS1
Synonyms:	GST2
ORF Names:	CG8938

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May be involved in the detoxification of metabolites produced during cellular division and morphogenesis.
Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.5
Subunit structure	Homodimer. Ref.5
Developmental stage	Expressed throughout development with highest levels being observed in nonfeeding stages, i.e. During embryonic and pupal development.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from direct assay PubMed 22082028. Source: FlyBase
Molecular_function	glutathione peroxidase activity Inferred from direct assay PubMed 11358508. Source: FlyBase glutathione transferase activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 249

249

Glutathione S-transferase S1

PRO_0000185917

Regions

Domain

48 – 125

78

GST N-terminal

Domain

127 – 249

123

GST C-terminal

Region

96 – 97

2

Glutathione binding

Region

109 – 110

2

Glutathione binding

Sites

Binding site

54

1

Glutathione

Binding site

85

1

Glutathione

Binding site

89

1

Glutathione By similarity

Experimental info

Sequence conflict

61 – 70

10

AEPLRYLFAY → PSPCATCSD in AAA28596. Ref.1

Sequence conflict

79 – 85

7

RVTRDEW → AHPRRV in AAA28596. Ref.1

Sequence conflict

224

1

L → V in AAA28596. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

249

Helix Strand Turn

Details...

Beta strand

50 – 58

9

Helix

59 – 61

3

Helix

62 – 71

10

Beta strand

76 – 80

5

Turn

82 – 84

3

Helix

85 – 88

4

Helix

89 – 91

3

Helix

93 – 95

3

Beta strand

99 – 102

4

Beta strand

105 – 108

4

Helix

110 – 121

12

Helix

128 – 152

25

Helix

157 – 169

13

Helix

171 – 185

15

Beta strand

188 – 191

4

Helix

197 – 213

17

Turn

217 – 220

4

Helix

222 – 232

11

Helix

235 – 243

9

Sequences

	Sequence		Length	Mass (Da)
	P41043 [UniParc]. Last modified January 27, 2003. Version 2. Checksum: 11AB417F550859BD	FASTA	249	27,614
	10 20 30 40 50 60 MADEAQAPPA EGAPPAEGEA PPPAEGAEGA VEGGEAAPPA EPAEPIKHSY TLFYFNVKAL 70 80 90 100 110 120 AEPLRYLFAY GNQEYEDVRV TRDEWPALKP TMPMGQMPVL EVDGKRVHQS ISMARFLAKT 130 140 150 160 170 180 VGLCGATPWE DLQIDIVVDT INDFRLKIAV VSYEPEDEIK EKKLVTLNAE VIPFYLEKLE 190 200 210 220 230 240 QTVKDNDGHL ALGKLTWADV YFAGITDYMN YMVKRDLLEP YPALRGVVDA VNALEPIKAW IEKRPVTEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a Drosophila gene encoding glutathione S-transferase." Beall C., Fyrberg C., Song S., Fyrberg E. Biochem. Genet. 30:515-527(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products." Agianian B., Tucker P.A., Schouten A., Leonard K., Bullard B., Gros P. J. Mol. Biol. 326:151-165(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M95198 mRNA. Translation: AAA28596.1.
AE013599 Genomic DNA. Translation: AAF57901.1.
AY118328 mRNA. Translation: AAM48357.1.

PIR

A48982.

RefSeq

NP_523767.2. NM_079043.3.
NP_725653.1. NM_166216.2.
NP_725654.1. NM_166217.3.

UniGene

Dm.19945.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M0U	X-ray	1.75	A/B	1-249	[»]

ProteinModelPortal

P41043.

SMR

P41043. Positions 47-249.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-21396N.

IntAct

P41043. 1 interaction.

MINT

MINT-1625589.

Proteomic databases

PaxDb

P41043.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0087005; FBpp0086156; FBgn0010226.
FBtr0087006; FBpp0086157; FBgn0010226.
FBtr0100258; FBpp0099646; FBgn0010226.

GeneID

36927.

KEGG

dme:Dmel_CG8938.

Organism-specific databases

CTD

36927.

FlyBase

FBgn0010226. GstS1.

Phylogenomic databases

eggNOG

NOG122057.

GeneTree

ENSGT00550000074559.

InParanoid

P41043.

KO

K00799.

OMA

YEPEDEI.

OrthoDB

EOG4N02WZ.

PhylomeDB

P41043.

Gene expression databases

Bgee

P41043.

GermOnline

CG8938. Drosophila melanogaster.

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...

Other

ChiTaRS

GstS1. drosophila.

EvolutionaryTrace

P41043.

GenomeRNAi

36927.

NextBio

801072.

Entry information

Entry name

GST1_DROME

Accession

Primary (citable) accession number: P41043
Secondary accession number(s): Q0E945, Q9V7Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 27, 2003
Last modified:	April 3, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project