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Protein

Glutathione S-transferase D5

Gene

GstD5

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.By similarity

Catalytic activityi

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

GO - Molecular functioni

  • glutathione transferase activity Source: FlyBase

GO - Biological processi

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

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase D5 (EC:2.5.1.18)
Short name:
DmGST24
Gene namesi
Name:GstD5
Synonyms:gstD24
ORF Names:CG12242
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010041. GstD5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 216216Glutathione S-transferase D5PRO_0000185957Add
BLAST

Proteomic databases

PaxDbiQ9VG95.

Expressioni

Gene expression databases

BgeeiQ9VG95.
ExpressionAtlasiQ9VG95. differential.
GenevisibleiQ9VG95. DM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi71335. 5 interactions.
STRINGi7227.FBpp0082044.

Structurei

3D structure databases

ProteinModelPortaliQ9VG95.
SMRiQ9VG95. Positions 1-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8080GST N-terminalAdd
BLAST
Domaini86 – 207122GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 523Glutathione bindingBy similarity
Regioni64 – 663Glutathione bindingBy similarity

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.
InParanoidiQ9VG95.
KOiK00799.
OMAiPASAPCR.
OrthoDBiEOG7V1FRJ.
PhylomeDBiQ9VG95.

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.
PF13417. GST_N_3. 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.

Q9VG95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFYYSPRGS GCRTVIMVAK ALGVKLNMKL LNTLEKDQLK PEFVKLNPQH
60 70 80 90 100
TIPTLVDNGF SIWESRAIAV YLVEKYGKDD TLFPKDPKKQ ALVNQRLYFD
110 120 130 140 150
MGTLYDSFAK YYYPLFHTGK PGSDEDFKKI ESSFEYLNIF LEGQNYVAGD
160 170 180 190 200
HLTVADIAIL STVSTFEIFD FDLNKYPNVA RWYANAKKVT PGWEENWKGA
210
VELKGVFDAR QAAAKQ
Length:216
Mass (Da):24,713
Last modified:December 1, 2000 - v2
Checksum:i9136816534D39A18
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAF54790.3.
PIRiC46681.
RefSeqiNP_524914.3. NM_080175.3.

Genome annotation databases

EnsemblMetazoaiFBtr0082572; FBpp0082044; FBgn0010041.
GeneIDi48338.
KEGGidme:Dmel_CG12242.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAF54790.3.
PIRiC46681.
RefSeqiNP_524914.3. NM_080175.3.

3D structure databases

ProteinModelPortaliQ9VG95.
SMRiQ9VG95. Positions 1-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi71335. 5 interactions.
STRINGi7227.FBpp0082044.

Proteomic databases

PaxDbiQ9VG95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082572; FBpp0082044; FBgn0010041.
GeneIDi48338.
KEGGidme:Dmel_CG12242.

Organism-specific databases

CTDi48338.
FlyBaseiFBgn0010041. GstD5.

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00540000069741.
InParanoidiQ9VG95.
KOiK00799.
OMAiPASAPCR.
OrthoDBiEOG7V1FRJ.
PhylomeDBiQ9VG95.

Miscellaneous databases

GenomeRNAii48338.
NextBioi839340.
PROiQ9VG95.

Gene expression databases

BgeeiQ9VG95.
ExpressionAtlasiQ9VG95. differential.
GenevisibleiQ9VG95. DM.

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.
PF13417. GST_N_3. 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. "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].
  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.

Entry informationi

Entry nameiGSTT5_DROME
AccessioniPrimary (citable) accession number: Q9VG95
Secondary accession number(s): Q9TX92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: June 24, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.