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Protein

Bifunctional glutathionylspermidine synthetase/amidase

Gene

gss

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. May act synergistically with glutaredoxin to regulate the redox environment and defend against oxidative damage.By similarity

Catalytic activityi

Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate.By similarity
Glutathionylspermidine + H2O = glutathione + spermidine.By similarity

Enzyme regulationi

When exposed to oxidative stress, Gsp amidase activity is transiently inhibited in vivo by oxidation of the catalytic Cys-59 thiol to sulfenic acid; this modification does not affect Gsp synthetase activity.By similarity

Pathwayi: glutathione metabolism

This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

Pathwayi: spermidine metabolism

This protein is involved in the pathway spermidine metabolism, which is part of Amine and polyamine metabolism.
View all proteins of this organism that are known to be involved in the pathway spermidine metabolism and in Amine and polyamine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei58GspBy similarity1
Active sitei59S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediateBy similarity1
Binding sitei64GspBy similarity1
Sitei131Increases nucleophilicity of active site Cys; for amidase activityBy similarity1
Binding sitei149GspBy similarity1
Binding sitei316GlutathioneBy similarity1
Sitei316Transition state stabilizer; for synthetase activityBy similarity1
Metal bindingi318Magnesium 1By similarity1
Metal bindingi330Magnesium 1By similarity1
Metal bindingi330Magnesium 2By similarity1
Metal bindingi332Magnesium 2By similarity1
Binding sitei335GlutathioneBy similarity1
Binding sitei391SpermidineBy similarity1
Binding sitei392GlutathioneBy similarity1
Binding sitei446GlutathioneBy similarity1
Binding sitei498ATPBy similarity1
Binding sitei533ATPBy similarity1
Binding sitei582ATPBy similarity1
Binding sitei610SpermidineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi316 – 318ATPBy similarity3
Nucleotide bindingi539 – 540ATPBy similarity2
Nucleotide bindingi568 – 571ATPBy similarity4
Nucleotide bindingi603 – 605ATPBy similarity3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00204.
UPA00819.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional glutathionylspermidine synthetase/amidase
Short name:
GspSA
Including the following 2 domains:
Glutathionylspermidine amidase (EC:3.5.1.78By similarity)
Short name:
Gsp amidase
Alternative name(s):
Glutathionylspermidine amidohydrolase [spermidine-forming]
Glutathionylspermidine synthetase (EC:6.3.1.8By similarity)
Short name:
Gsp synthetase
Alternative name(s):
Glutathione:spermidine ligase [ADP-forming]
Gsp synthase
Gene namesi
Name:gss
Synonyms:gsp
Ordered Locus Names:SF3035, S3236
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000704442 – 619Bifunctional glutathionylspermidine synthetase/amidaseAdd BLAST618

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei59Cysteine sulfenic acid (-SOH); transientBy similarity1

Post-translational modificationi

Oxidation of Cys-59 to sulfenic acid during oxidative stress selectively inhibits the amidase activity.By similarity

Keywords - PTMi

Oxidation

Proteomic databases

PaxDbiP0AES1.
PRIDEiP0AES1.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi198214.SF3035.

Structurei

3D structure databases

ProteinModelPortaliP0AES1.
SMRiP0AES1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 176Peptidase C51PROSITE-ProRule annotationAdd BLAST143

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 195Gsp amidaseAdd BLAST194
Regioni78 – 81Gsp bindingBy similarity4
Regioni196 – 205Linker10
Regioni206 – 619Gsp synthetaseAdd BLAST414

Domaini

The two activities reside in distinct domains (N-terminal amidase and C-terminal synthetase). The two domains expressed independently are folded and functional (By similarity).By similarity

Sequence similaritiesi

In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.Curated
Contains 1 peptidase C51 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4106032. Bacteria.
COG0754. LUCA.
HOGENOMiHOG000124980.
KOiK01460.
OMAiPNHRYLL.

Family and domain databases

InterProiIPR007921. CHAP_dom.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS50911. CHAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0AES1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKGTTSQDA PFGTLLGYAP GGVAIYSSDY SSLDPQEYED DAVFRSYIDD
60 70 80 90 100
EYMGHKWQCV EFARRFLFLN YGVVFTDVGM AWEIFSLRFL REVVNDNILP
110 120 130 140 150
LQAFPNGSPR APVAGALLIW DKGGEFKDTG HVAIITQLHG NKVRIAEQNV
160 170 180 190 200
IHSPLPQGQQ WTRELEMVVE NGCYTLKDTF DDTTILGWMI QTEDTEYSLP
210 220 230 240 250
QPEIAGELLK ISGARLENKG QFDGKWLDEK DPLQNAYVQA NGQVINQDPY
260 270 280 290 300
HYYTITESAE QELIKATNEL HLMYLHATDK VLKDDNLLAL FDIPKILWPR
310 320 330 340 350
LRLSWQRRRH HMITGRMDFC MDERGLKVYE YNADSASCHT EAGLILERWA
360 370 380 390 400
EQGYKGNGFN PAEGLINELA GAWKHSRARP FVHIMQDKDI EENYHAQFME
410 420 430 440 450
QALHQAGFET RILRGLDELG WDAAGQLIDG EGRLVNCVWK TWAWETAFDQ
460 470 480 490 500
IREVSDREFA AVPIRTGHPQ NEVRLIDVLL RPEVLVFEPL WTVIPGNKAI
510 520 530 540 550
LPILWSLFPH HRYLLDTDFT VNDELVKTGY AVKPIAGRCG SNIDLVSHHE
560 570 580 590 600
EVLDKTSGKF AEQKNIYQQL WCLPKVDGKY IQVCTFTVGG NYGGTCLRGD
610
ESLVIKKESD IEPLIVVKK
Length:619
Mass (Da):70,532
Last modified:December 20, 2005 - v1
Checksum:i07FB43D8A0B2933C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN44513.2.
AE014073 Genomic DNA. Translation: AAP18324.1.
RefSeqiNP_708806.2. NC_004337.2.
WP_001297309.1. NZ_LVJC01000027.1.

Genome annotation databases

EnsemblBacteriaiAAN44513; AAN44513; SF3035.
AAP18324; AAP18324; S3236.
GeneIDi1026646.
KEGGisfl:SF3035.
sft:NCTC1_03289.
sfx:S3236.
PATRICi18708196. VBIShiFle31049_3546.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN44513.2.
AE014073 Genomic DNA. Translation: AAP18324.1.
RefSeqiNP_708806.2. NC_004337.2.
WP_001297309.1. NZ_LVJC01000027.1.

3D structure databases

ProteinModelPortaliP0AES1.
SMRiP0AES1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF3035.

Proteomic databases

PaxDbiP0AES1.
PRIDEiP0AES1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN44513; AAN44513; SF3035.
AAP18324; AAP18324; S3236.
GeneIDi1026646.
KEGGisfl:SF3035.
sft:NCTC1_03289.
sfx:S3236.
PATRICi18708196. VBIShiFle31049_3546.

Phylogenomic databases

eggNOGiENOG4106032. Bacteria.
COG0754. LUCA.
HOGENOMiHOG000124980.
KOiK01460.
OMAiPNHRYLL.

Enzyme and pathway databases

UniPathwayiUPA00204.
UPA00819.

Family and domain databases

InterProiIPR007921. CHAP_dom.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS50911. CHAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSP_SHIFL
AccessioniPrimary (citable) accession number: P0AES1
Secondary accession number(s): P43675
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.