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Protein

Glutathione S-transferase 1-1

Gene

GstD1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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. Has DDT dehydrochlorinase activity.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication
1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Glutathione1 Publication

GO - Molecular functioni

  1. DDT-dehydrochlorinase activity Source: FlyBase
  2. glutathione transferase activity Source: FlyBase

GO - Biological processi

  1. glutathione metabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 1-1 (EC:2.5.1.18, EC:4.5.1.1)
Alternative name(s):
DDT-dehydrochlorinase
GST class-theta
Gene namesi
Name:GstD1
Synonyms:GST, Gst1
ORF Names:CG10045
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0001149. GstD1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 209209Glutathione S-transferase 1-1PRO_0000185947Add
BLAST

Proteomic databases

PaxDbiP20432.
PRIDEiP20432.

Expressioni

Gene expression databases

BgeeiP20432.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi66612. 15 interactions.
DIPiDIP-17237N.
IntActiP20432. 4 interactions.
MINTiMINT-323021.

Structurei

Secondary structure

1
209
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Helixi11 – 2313Combined sources
Beta strandi28 – 314Combined sources
Helixi34 – 363Combined sources
Helixi38 – 403Combined sources
Helixi42 – 454Combined sources
Beta strandi55 – 584Combined sources
Beta strandi61 – 644Combined sources
Helixi66 – 7712Combined sources
Beta strandi79 – 813Combined sources
Helixi88 – 10316Combined sources
Helixi105 – 11915Combined sources
Helixi125 – 14117Combined sources
Turni142 – 1443Combined sources
Beta strandi146 – 1527Combined sources
Helixi155 – 16915Combined sources
Helixi174 – 1763Combined sources
Helixi178 – 19013Combined sources
Helixi194 – 20411Combined sources
Helixi205 – 2073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EINX-ray1.13A1-209[»]
3MAKX-ray1.80A1-209[»]
ProteinModelPortaliP20432.
SMRiP20432. Positions 2-208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20432.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8181GST N-terminalAdd
BLAST
Domaini87 – 208122GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 533Glutathione binding
Regioni65 – 673Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Theta family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00540000069741.
InParanoidiP20432.
KOiK00799.
OMAiYTRLAHE.
OrthoDBiEOG7V1FRJ.
PhylomeDBiP20432.

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.

P20432-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDFYYLPGS SPCRSVIMTA KAVGVELNKK LLNLQAGEHL KPEFLKINPQ
60 70 80 90 100
HTIPTLVDNG FALWESRAIQ VYLVEKYGKT DSLYPKCPKK RAVINQRLYF
110 120 130 140 150
DMGTLYQSFA NYYYPQVFAK APADPEAFKK IEAAFEFLNT FLEGQDYAAG
160 170 180 190 200
DSLTVADIAL VATVSTFEVA KFEISKYANV NRWYENAKKV TPGWEENWAG

CLEFKKYFE
Length:209
Mass (Da):23,866
Last modified:January 31, 1991 - v1
Checksum:i4AD8E237CCF804F2
GO

Sequence cautioni

The sequence AAM52032.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14233 mRNA. Translation: CAA32449.1.
S51044 mRNA. Translation: AAA04220.1.
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAF54786.1.
AE014297 Genomic DNA. Translation: ABC66168.1.
AY121705 mRNA. Translation: AAM52032.1. Different initiation.
PIRiA34798. XUFF11.
RefSeqiNP_001034042.1. NM_001038953.2.
NP_524326.1. NM_079602.5.
UniGeneiDm.2439.

Genome annotation databases

EnsemblMetazoaiFBtr0082607; FBpp0082077; FBgn0001149.
FBtr0100410; FBpp0099824; FBgn0001149.
GeneIDi41503.
KEGGidme:Dmel_CG10045.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14233 mRNA. Translation: CAA32449.1.
S51044 mRNA. Translation: AAA04220.1.
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAF54786.1.
AE014297 Genomic DNA. Translation: ABC66168.1.
AY121705 mRNA. Translation: AAM52032.1. Different initiation.
PIRiA34798. XUFF11.
RefSeqiNP_001034042.1. NM_001038953.2.
NP_524326.1. NM_079602.5.
UniGeneiDm.2439.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EINX-ray1.13A1-209[»]
3MAKX-ray1.80A1-209[»]
ProteinModelPortaliP20432.
SMRiP20432. Positions 2-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66612. 15 interactions.
DIPiDIP-17237N.
IntActiP20432. 4 interactions.
MINTiMINT-323021.

Proteomic databases

PaxDbiP20432.
PRIDEiP20432.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082607; FBpp0082077; FBgn0001149.
FBtr0100410; FBpp0099824; FBgn0001149.
GeneIDi41503.
KEGGidme:Dmel_CG10045.

Organism-specific databases

CTDi41503.
FlyBaseiFBgn0001149. GstD1.

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00540000069741.
InParanoidiP20432.
KOiK00799.
OMAiYTRLAHE.
OrthoDBiEOG7V1FRJ.
PhylomeDBiP20432.

Miscellaneous databases

ChiTaRSiGstS1. fly.
EvolutionaryTraceiP20432.
GenomeRNAii41503.
NextBioi824191.

Gene expression databases

BgeeiP20432.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila glutathione S-transferase 1-1 shares a region of sequence homology with the maize glutathione S-transferase III."
    Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.
    Proc. Natl. Acad. Sci. U.S.A. 87:31-35(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-20.
    Strain: Oregon-R.
  2. "The Drosophila glutathione S-transferase 1-1 is encoded by an intronless gene at 87B."
    Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.
    Biochem. Biophys. Res. Commun. 178:1205-1211(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster."
    Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.
    J. Biol. Chem. 268:9737-9746(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  7. "Recognition and detoxification of the insecticide DDT by Drosophila melanogaster glutathione S-transferase D1."
    Low W.Y., Feil S.C., Ng H.L., Gorman M.A., Morton C.J., Pyke J., McConville M.J., Bieri M., Mok Y.F., Robin C., Gooley P.R., Parker M.W., Batterham P.
    J. Mol. Biol. 399:358-366(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.13 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION AS DDT DEHYDROCHLORINASE, CATALYTIC ACTIVITY, SUBUNIT.

Entry informationi

Entry nameiGSTT1_DROME
AccessioniPrimary (citable) accession number: P20432
Secondary accession number(s): Q4JFI6
, Q8MR98, Q9TX88, Q9VG99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1991
Last sequence update: January 31, 1991
Last modified: February 3, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Has a specific activity toward 1-chloro-2,4-dinitrobenzene comparable to that for the mammalian glutathione S-transferases but did not have as broad a substrate specificity pattern. Has no GSH peroxidase activity.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.