Reviewed, UniProtKB/Swiss-Prot P41043 (GST1_DROME)

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) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subunit structure	Homodimer By similarity.
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
Gene Ontology (GO)
Biological process	metabolic process Ref.1 Inferred by curator. Source: UniProtKB
Molecular function	glutathione peroxidase activity Inferred from direct assay. Source: FlyBase 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

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

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)
	P41043-1 [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: 1445191] [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: 10731132] [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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

PIR

A48982.

RefSeq

NP_523767.2.
NP_725653.1.
NP_725654.1.

UniGene

Dm.19945

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:21396N.

IntAct

P41043. 3 interactions.

Genome annotation databases

Ensembl

FBgn0010226. Drosophila melanogaster. [Contig view]

GeneID

36927.

KEGG

dme:Dmel_CG8938.

Organism-specific databases

FlyBase

FBgn0010226. GstS1.

Phylogenomic databases

HOGENOM

P41043.

OMA

P41043. SISMARF.

Enzyme and pathway databases

BioCyc

DMEL-XXX-02:DMEL-XXX-02-005099-MON.
DMEL-XXX-02:DMEL-XXX-02-005100-MON.
DMEL-XXX-02:DMEL-XXX-02-005101-MON.

BRENDA

2.5.1.18. 48.

Gene expression databases

ArrayExpress

P41043.

GermOnline

CG8938. Drosophila melanogaster.

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.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 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...

Other Resources

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:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project