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Protein

Glutathione S-transferase gliG

Gene

gliG

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).11 Publications

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.2 Publications

Pathwayi: Mycotoxin biosynthesis

This protein is involved in Mycotoxin biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in Mycotoxin biosynthesis.

GO - Molecular functioni

  • glutathione transferase activity Source: AspGD

GO - Biological processi

  • gliotoxin biosynthetic process Source: AspGD
  • mycotoxin biosynthetic process Source: AspGD
  • pathogenesis Source: UniProtKB-KW

Keywordsi

Molecular functionTransferase
Biological processVirulence

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18849

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase gliG1 Publication (EC:2.5.1.182 Publications)
Alternative name(s):
Gliotoxin biosynthesis protein G1 Publication
Gene namesi
Name:gliG1 Publication
ORF Names:AFUA_6G09690
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componentsi: Chromosome 6, Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:Afu6g09690

Pathology & Biotechi

Disruption phenotypei

Abrogates gliotoxin biosynthesis and leads to the accumulation of the shunt metabolite 6-benzyl-6-hydroxy-1-methoxy-3-methylene-piperazine-2,5-dione (PubMed:21513890).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004377241 – 240Glutathione S-transferase gliGAdd BLAST240

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUBP00007378

Structurei

3D structure databases

ProteinModelPortaliA4GYZ0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 98GST N-terminalPROSITE-ProRule annotationAdd BLAST84
Domaini104 – 237GST C-terminalPROSITE-ProRule annotationAdd BLAST134

Sequence similaritiesi

Belongs to the GST superfamily.Curated

Phylogenomic databases

HOGENOMiHOG000187231
InParanoidiA4GYZ0
KOiK22119
OMAiAKYWLYF
OrthoDBiEOG092C4LON

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
PF00043 GST_C, 1 hit
PF13417 GST_N_3, 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.

A4GYZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSERPSDLVV NRLVLFVVKG TATSTHNTVK PLILLEELGV PHDIYVVEKV
60 70 80 90 100
SAPWFSEINP HKMVPAILDR SPDGRDTLRA WESTSTLMYI ADAYDKDGTL
110 120 130 140 150
GGRNVQERSE INNWLTLHTA ALGPTAKYWL YFYKLHPEKL PKTIEKLRSN
160 170 180 190 200
ITVQYDILER RLNEPGQQYL ALKDRPTIAD IATLPFAMKS TAELFGLEFE
210 220 230 240
KWPKLQEWSV RMGEREAVKR AWQRVAGFGH GEKEYGMLEA
Length:240
Mass (Da):27,470
Last modified:April 17, 2007 - v1
Checksum:i5352BD3FFD7D1A4B
GO

Sequence cautioni

The sequence AAW03304 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY838877 Genomic DNA Translation: AAW03304.1 Sequence problems.
AAHF01000006 Genomic DNA Translation: EAL88820.2
RefSeqiXP_750858.2, XM_745765.2

Genome annotation databases

EnsemblFungiiCADAFUAT00001942; CADAFUAP00001942; CADAFUAG00001942
GeneIDi3508163
KEGGiafm:AFUA_6G09690

Similar proteinsi

Entry informationi

Entry nameiGLIG_ASPFU
AccessioniPrimary (citable) accession number: A4GYZ0
Secondary accession number(s): Q5MBU2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2016
Last sequence update: April 17, 2007
Last modified: April 25, 2018
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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