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P20432 (GSTT1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GstD1
Synonyms:GST, Gst1
ORF Names:CG10045
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has DDT dehydrochlorinase activity. Ref.7

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.7

1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride. Ref.7

Subunit structure

Homodimer. Ref.7

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.

Sequence similarities

Belongs to the GST superfamily. Theta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209Glutathione S-transferase 1-1
PRO_0000185947

Regions

Domain1 – 8181GST N-terminal
Domain87 – 208122GST C-terminal
Region51 – 533Glutathione binding
Region65 – 673Glutathione binding

Sites

Binding site101Glutathione

Secondary structure

....................................... 209
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20432 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 4AD8E237CCF804F2

FASTA20923,866
        10         20         30         40         50         60 
MVDFYYLPGS SPCRSVIMTA KAVGVELNKK LLNLQAGEHL KPEFLKINPQ HTIPTLVDNG 

        70         80         90        100        110        120 
FALWESRAIQ VYLVEKYGKT DSLYPKCPKK RAVINQRLYF DMGTLYQSFA NYYYPQVFAK 

       130        140        150        160        170        180 
APADPEAFKK IEAAFEFLNT FLEGQDYAAG DSLTVADIAL VATVSTFEVA KFEISKYANV 

       190        200 
NRWYENAKKV TPGWEENWAG CLEFKKYFE 

« Hide

References

« Hide 'large scale' references
[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(1990) [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(1991) [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(1993) [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. expand/collapse author list , 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.
[5]"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. expand/collapse author list , 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.
[6]"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: 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(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.13 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION AS DDT DEHYDROCHLORINASE, CATALYTIC ACTIVITY, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRXUFF11. A34798.
RefSeqNP_001034042.1. NM_001038953.1.
NP_524326.1. NM_079602.4.
UniGeneDm.2439.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EINX-ray1.13A1-209[»]
3MAKX-ray1.80A1-209[»]
ProteinModelPortalP20432.
SMRP20432. Positions 2-208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66612. 15 interactions.
DIPDIP-17237N.
IntActP20432. 2 interactions.
MINTMINT-323021.

Proteomic databases

PaxDbP20432.
PRIDEP20432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082607; FBpp0082077; FBgn0001149.
FBtr0100410; FBpp0099824; FBgn0001149.
GeneID41503.
KEGGdme:Dmel_CG10045.

Organism-specific databases

CTD41503.
FlyBaseFBgn0001149. GstD1.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00540000069741.
InParanoidP20432.
KOK00799.
OMAYTRLAHE.
OrthoDBEOG7V1FRJ.
PhylomeDBP20432.

Gene expression databases

BgeeP20432.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20432.
GenomeRNAi41503.
NextBio824191.

Entry information

Entry nameGSTT1_DROME
AccessionPrimary (citable) accession number: P20432
Secondary accession number(s): Q4JFI6 expand/collapse secondary AC list , Q8MR98, Q9TX88, Q9VG99
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 19, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase