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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).By similarity

Catalytic activityi

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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581GspBy similarity
Active sitei59 – 591S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediateBy similarity
Binding sitei64 – 641GspBy similarity
Sitei131 – 1311Increases nucleophilicity of active site Cys; for amidase activityBy similarity
Binding sitei149 – 1491GspBy similarity
Binding sitei316 – 3161GlutathioneBy similarity
Sitei316 – 3161Transition state stabilizer; for synthetase activityBy similarity
Metal bindingi318 – 3181Magnesium 1By similarity
Metal bindingi330 – 3301Magnesium 1By similarity
Metal bindingi330 – 3301Magnesium 2By similarity
Metal bindingi332 – 3321Magnesium 2By similarity
Binding sitei335 – 3351GlutathioneBy similarity
Binding sitei391 – 3911SpermidineBy similarity
Binding sitei392 – 3921GlutathioneBy similarity
Binding sitei446 – 4461GlutathioneBy similarity
Binding sitei498 – 4981ATPBy similarity
Binding sitei533 – 5331ATPBy similarity
Binding sitei582 – 5821ATPBy similarity
Binding sitei610 – 6101SpermidineBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi316 – 3183ATPBy similarity
Nucleotide bindingi539 – 5402ATPBy similarity
Nucleotide bindingi568 – 5714ATPBy similarity
Nucleotide bindingi603 – 6053ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutathionylspermidine amidase activity Source: UniProtKB-EC
  3. glutathionylspermidine synthase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glutathione metabolic process Source: UniProtKB-UniPathway
  2. spermidine metabolic process Source: UniProtKB-UniPathway
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:3.5.1.78)
Short name:
Gsp amidase
Alternative name(s):
Glutathionylspermidine amidohydrolase [spermidine-forming]
Glutathionylspermidine synthetase (EC:6.3.1.8)
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002673 Componenti: Chromosome UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 619618Bifunctional glutathionylspermidine synthetase/amidasePRO_0000070444Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Cysteine sulfenic acid (-SOH); transientBy similarity

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. Positions 8-618.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 176143Peptidase C51PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 195194Gsp amidaseAdd
BLAST
Regioni78 – 814Gsp bindingBy similarity
Regioni196 – 20510Linker
Regioni206 – 619414Gsp synthetaseAdd
BLAST

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

eggNOGiCOG0754.
HOGENOMiHOG000124980.
KOiK01460.
OMAiYHALFIQ.
OrthoDBiEOG66XB93.

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.
NP_838514.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN44513; AAN44513; SF3035.
AAP18324; AAP18324; S3236.
GeneIDi1026646.
1079490.
KEGGisfl:SF3035.
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.
NP_838514.1. NC_004741.1.

3D structure databases

ProteinModelPortaliP0AES1.
SMRiP0AES1. Positions 8-618.
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.
1079490.
KEGGisfl:SF3035.
sfx:S3236.
PATRICi18708196. VBIShiFle31049_3546.

Phylogenomic databases

eggNOGiCOG0754.
HOGENOMiHOG000124980.
KOiK01460.
OMAiYHALFIQ.
OrthoDBiEOG66XB93.

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...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

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: January 7, 2015
This is version 65 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

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.