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P41043

- GST1_DROME

UniProt

P41043 - GST1_DROME

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Protein
Glutathione S-transferase S1
Gene
GstS1, GST2, CG8938
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541Glutathione
Binding sitei85 – 851Glutathione
Binding sitei89 – 891Glutathione By similarity

GO - Molecular functioni

  1. glutathione peroxidase activity Source: FlyBase
  2. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione metabolic process Source: FlyBase
  2. metabolic process Source: UniProtKB
  3. oxidation-reduction process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_207120. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_209269. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase S1 (EC:2.5.1.18)
Alternative name(s):
GST class-sigma 1
Glutathione S-transferase 2
Gene namesi
Name:GstS1
Synonyms:GST2
ORF Names:CG8938
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0010226. GstS1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Glutathione S-transferase S1
PRO_0000185917Add
BLAST

Proteomic databases

PaxDbiP41043.

Expressioni

Developmental stagei

Expressed throughout development with highest levels being observed in nonfeeding stages, i.e. During embryonic and pupal development.

Gene expression databases

BgeeiP41043.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi62625. 28 interactions.
DIPiDIP-21396N.
IntActiP41043. 1 interaction.
MINTiMINT-1625589.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 589
Helixi59 – 613
Helixi62 – 7110
Beta strandi76 – 805
Turni82 – 843
Helixi85 – 884
Helixi89 – 913
Helixi93 – 953
Beta strandi99 – 1024
Beta strandi105 – 1084
Helixi110 – 12112
Helixi128 – 15225
Helixi157 – 16913
Helixi171 – 18515
Beta strandi188 – 1914
Helixi197 – 21317
Turni217 – 2204
Helixi222 – 23211
Helixi235 – 2439

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M0UX-ray1.75A/B1-249[»]
ProteinModelPortaliP41043.
SMRiP41043. Positions 47-249.

Miscellaneous databases

EvolutionaryTraceiP41043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 12578GST N-terminal
Add
BLAST
Domaini127 – 249123GST C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 972Glutathione binding
Regioni109 – 1102Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Sigma family.

Phylogenomic databases

eggNOGiNOG122057.
GeneTreeiENSGT00670000097856.
InParanoidiP41043.
KOiK00799.
OrthoDBiEOG78WKT1.
PhylomeDBiP41043.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41043-1 [UniParc]FASTAAdd to Basket

« Hide

MADEAQAPPA EGAPPAEGEA PPPAEGAEGA VEGGEAAPPA EPAEPIKHSY    50
TLFYFNVKAL AEPLRYLFAY GNQEYEDVRV TRDEWPALKP TMPMGQMPVL 100
EVDGKRVHQS ISMARFLAKT VGLCGATPWE DLQIDIVVDT INDFRLKIAV 150
VSYEPEDEIK EKKLVTLNAE VIPFYLEKLE QTVKDNDGHL ALGKLTWADV 200
YFAGITDYMN YMVKRDLLEP YPALRGVVDA VNALEPIKAW IEKRPVTEV 249
Length:249
Mass (Da):27,614
Last modified:January 27, 2003 - v2
Checksum:i11AB417F550859BD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 7010AEPLRYLFAY → PSPCATCSD in AAA28596. 1 Publication
Sequence conflicti79 – 857RVTRDEW → AHPRRV in AAA28596. 1 Publication
Sequence conflicti224 – 2241L → V in AAA28596. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M95198 mRNA. Translation: AAA28596.1.
AE013599 Genomic DNA. Translation: AAF57901.1.
AY118328 mRNA. Translation: AAM48357.1.
PIRiA48982.
RefSeqiNP_523767.2. NM_079043.3.
NP_725653.1. NM_166216.2.
NP_725654.1. NM_166217.3.
UniGeneiDm.19945.

Genome annotation databases

EnsemblMetazoaiFBtr0087005; FBpp0086156; FBgn0010226.
FBtr0087006; FBpp0086157; FBgn0010226.
FBtr0100258; FBpp0099646; FBgn0010226.
GeneIDi36927.
KEGGidme:Dmel_CG8938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M95198 mRNA. Translation: AAA28596.1 .
AE013599 Genomic DNA. Translation: AAF57901.1 .
AY118328 mRNA. Translation: AAM48357.1 .
PIRi A48982.
RefSeqi NP_523767.2. NM_079043.3.
NP_725653.1. NM_166216.2.
NP_725654.1. NM_166217.3.
UniGenei Dm.19945.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M0U X-ray 1.75 A/B 1-249 [» ]
ProteinModelPortali P41043.
SMRi P41043. Positions 47-249.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62625. 28 interactions.
DIPi DIP-21396N.
IntActi P41043. 1 interaction.
MINTi MINT-1625589.

Proteomic databases

PaxDbi P41043.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0087005 ; FBpp0086156 ; FBgn0010226 .
FBtr0087006 ; FBpp0086157 ; FBgn0010226 .
FBtr0100258 ; FBpp0099646 ; FBgn0010226 .
GeneIDi 36927.
KEGGi dme:Dmel_CG8938.

Organism-specific databases

CTDi 36927.
FlyBasei FBgn0010226. GstS1.

Phylogenomic databases

eggNOGi NOG122057.
GeneTreei ENSGT00670000097856.
InParanoidi P41043.
KOi K00799.
OrthoDBi EOG78WKT1.
PhylomeDBi P41043.

Enzyme and pathway databases

Reactomei REACT_207120. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_209269. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSi GstS1. drosophila.
EvolutionaryTracei P41043.
GenomeRNAii 36927.
NextBioi 801072.

Gene expression databases

Bgeei P41043.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiGST1_DROME
AccessioniPrimary (citable) accession number: P41043
Secondary accession number(s): Q0E945, Q9V7Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 27, 2003
Last modified: September 3, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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