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Protein

Putative glutathione S-transferase alpha-3

Gene

gsta3

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei8GlutathioneBy similarity1

GO - Molecular functioni

GO - Biological processi

  • response to curcumin Source: dictyBase

Keywordsi

Molecular functionTransferase

Names & Taxonomyi

Protein namesi
Recommended name:
Putative glutathione S-transferase alpha-3 (EC:2.5.1.18)
Alternative name(s):
GST class-alpha 3
Gene namesi
Name:gsta3
ORF Names:DDB_G0280317
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyostelidsDictyostelialesDictyosteliaceaeDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0280317

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00003507402 – 204Putative glutathione S-transferase alpha-3Add BLAST203

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ54VI4

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB0231429

Structurei

3D structure databases

ProteinModelPortaliQ54VI4
SMRiQ54VI4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 79GST N-terminalAdd BLAST78
Domaini81 – 202GST C-terminalAdd BLAST122

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 50Glutathione bindingBy similarity2
Regioni63 – 64Glutathione bindingBy similarity2

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.Curated

Phylogenomic databases

eggNOGiENOG41103AU LUCA
InParanoidiQ54VI4
KOiK04097
OMAiKPTWADV
PhylomeDBiQ54VI4

Family and domain databases

InterProiView protein in InterPro
IPR010987 Glutathione-S-Trfase_C-like
IPR036282 Glutathione-S-Trfase_C_sf
IPR004045 Glutathione_S-Trfase_N
IPR004046 GST_C
IPR036249 Thioredoxin-like_sf
PfamiView protein in Pfam
PF14497 GST_C_3, 1 hit
PF02798 GST_N, 1 hit
SUPFAMiSSF47616 SSF47616, 1 hit
SSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS50405 GST_CTER, 1 hit
PS50404 GST_NTER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q54VI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKPQLSYFK VRALGQFPRV LLSYLSIDYD NNYIDKIDEN IIDDLKYGQL
60 70 80 90 100
PLYTDSNGFK LVQSMAISKY IASQHDFVGK TPEEKALVDE TLAAVNIDVF
110 120 130 140 150
TFIIRVFRGV EEKEKIQEII IPRFFAKWNQ ILGEKKYLAG GNSYTLADLY
160 170 180 190 200
VYVAYEYIGY VLPFAADLLY NGKFPHLDSL KEHFESNKGV AEYLKNRPIT

ERKI
Length:204
Mass (Da):23,606
Last modified:May 24, 2005 - v1
Checksum:i16D7B61EDC21DCDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000035 Genomic DNA Translation: EAL67385.1
RefSeqiXP_641371.1, XM_636279.1

Genome annotation databases

EnsemblProtistsiEAL67385; EAL67385; DDB_G0280317
GeneIDi8622505
KEGGiddi:DDB_G0280317

Similar proteinsi

Entry informationi

Entry nameiGSTA3_DICDI
AccessioniPrimary (citable) accession number: Q54VI4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: May 24, 2005
Last modified: March 28, 2018
This is version 82 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health