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Protein

Putative glutathione S-transferase alpha-1

Gene

gsta1

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 sitei10GlutathioneBy similarity1
Binding sitei44GlutathioneBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionTransferase

Names & Taxonomyi

Protein namesi
Recommended name:
Putative glutathione S-transferase alpha-1 (EC:2.5.1.18)
Alternative name(s):
GST class-alpha 1
Gene namesi
Name:gsta1
ORF Names:DDB_G0268138
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyostelidsDictyostelialesDictyosteliaceaeDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 1, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0268138

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00003507382 – 202Putative glutathione S-transferase alpha-1Add BLAST201

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ55FF3

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB0231431

Structurei

3D structure databases

ProteinModelPortaliQ55FF3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 81GST N-terminalAdd BLAST78
Domaini83 – 200GST C-terminalAdd BLAST118

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni51 – 52Glutathione bindingBy similarity2
Regioni65 – 66Glutathione bindingBy similarity2

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.Curated

Phylogenomic databases

eggNOGiENOG410IN59 Eukaryota
ENOG410Y9SU LUCA
InParanoidiQ55FF3
KOiK00799
OMAiCPPAEKD
PhylomeDBiQ55FF3

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.

Q55FF3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTNKPSFSY FKVLVLGQLP RFTLNYFGTD FTDNYVESID DEFRKTLKFG
60 70 80 90 100
QLPLFVDSDG FRLTQTDAIC KYIAAKHDFL GKSIKERAIV DETIAAVHDD
110 120 130 140 150
VIIPGYKVGK GVEDKKVIDT IISRHFTTFE NVLAENKFIA GGDNYTLADL
160 170 180 190 200
YVFVAYHYYK HLGHSEKFQN KFPHLEALQA HFESNKGIAE YIKNRPDSGR

GI
Length:202
Mass (Da):23,063
Last modified:May 24, 2005 - v1
Checksum:iACA3DDF0E4738949
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000003 Genomic DNA Translation: EAL73522.1
RefSeqiXP_647580.1, XM_642488.1

Genome annotation databases

EnsemblProtistsiEAL73522; EAL73522; DDB_G0268138
GeneIDi8616392
KEGGiddi:DDB_G0268138

Similar proteinsi

Entry informationi

Entry nameiGSTA1_DICDI
AccessioniPrimary (citable) accession number: Q55FF3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: May 24, 2005
Last modified: March 28, 2018
This is version 91 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