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P0AES1 (GSP_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional glutathionylspermidine synthetase/amidase

Short name=GspSA

Including the following 2 domains:

  1. Glutathionylspermidine amidase
    Short name=Gsp amidase
    EC=3.5.1.78
    Alternative name(s):
    Glutathionylspermidine amidohydrolase [spermidine-forming]
  2. Glutathionylspermidine synthetase
    Short name=Gsp synthetase
    EC=6.3.1.8
    Alternative name(s):
    Glutathione:spermidine ligase [ADP-forming]
    Gsp synthase
Gene names
Name:gss
Synonyms:gsp
Ordered Locus Names:SF3035, S3236
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate.

Glutathionylspermidine + H2O = glutathione + spermidine.

Enzyme regulation

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.

Pathway

Sulfur metabolism; glutathione metabolism.

Amine and polyamine metabolism; spermidine metabolism.

Subunit structure

Homodimer By similarity.

Domain

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.

Post-translational modification

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

Sequence similarities

In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.

Contains 1 peptidase C51 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 619618Bifunctional glutathionylspermidine synthetase/amidase
PRO_0000070444

Regions

Domain34 – 176143Peptidase C51
Nucleotide binding316 – 3183ATP By similarity
Nucleotide binding539 – 5402ATP By similarity
Nucleotide binding568 – 5714ATP By similarity
Nucleotide binding603 – 6053ATP By similarity
Region2 – 195194Gsp amidase
Region78 – 814Gsp binding By similarity
Region196 – 20510Linker
Region206 – 619414Gsp synthetase

Sites

Active site591S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediate By similarity
Metal binding3181Magnesium 1 By similarity
Metal binding3301Magnesium 1 By similarity
Metal binding3301Magnesium 2 By similarity
Metal binding3321Magnesium 2 By similarity
Binding site581Gsp By similarity
Binding site641Gsp By similarity
Binding site1491Gsp By similarity
Binding site3161Glutathione By similarity
Binding site3351Glutathione By similarity
Binding site3911Spermidine By similarity
Binding site3921Glutathione By similarity
Binding site4461Glutathione By similarity
Binding site4981ATP By similarity
Binding site5331ATP By similarity
Binding site5821ATP By similarity
Binding site6101Spermidine By similarity
Site1311Increases nucleophilicity of active site Cys; for amidase activity By similarity
Site3161Transition state stabilizer; for synthetase activity By similarity

Amino acid modifications

Modified residue591Cysteine sulfenic acid (-SOH); transient By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AES1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 07FB43D8A0B2933C

FASTA61970,532
        10         20         30         40         50         60 
MSKGTTSQDA PFGTLLGYAP GGVAIYSSDY SSLDPQEYED DAVFRSYIDD EYMGHKWQCV 

        70         80         90        100        110        120 
EFARRFLFLN YGVVFTDVGM AWEIFSLRFL REVVNDNILP LQAFPNGSPR APVAGALLIW 

       130        140        150        160        170        180 
DKGGEFKDTG HVAIITQLHG NKVRIAEQNV IHSPLPQGQQ WTRELEMVVE NGCYTLKDTF 

       190        200        210        220        230        240 
DDTTILGWMI QTEDTEYSLP QPEIAGELLK ISGARLENKG QFDGKWLDEK DPLQNAYVQA 

       250        260        270        280        290        300 
NGQVINQDPY HYYTITESAE QELIKATNEL HLMYLHATDK VLKDDNLLAL FDIPKILWPR 

       310        320        330        340        350        360 
LRLSWQRRRH HMITGRMDFC MDERGLKVYE YNADSASCHT EAGLILERWA EQGYKGNGFN 

       370        380        390        400        410        420 
PAEGLINELA GAWKHSRARP FVHIMQDKDI EENYHAQFME QALHQAGFET RILRGLDELG 

       430        440        450        460        470        480 
WDAAGQLIDG EGRLVNCVWK TWAWETAFDQ IREVSDREFA AVPIRTGHPQ NEVRLIDVLL 

       490        500        510        520        530        540 
RPEVLVFEPL WTVIPGNKAI LPILWSLFPH HRYLLDTDFT VNDELVKTGY AVKPIAGRCG 

       550        560        570        580        590        600 
SNIDLVSHHE EVLDKTSGKF AEQKNIYQQL WCLPKVDGKY IQVCTFTVGG NYGGTCLRGD 

       610 
ESLVIKKESD IEPLIVVKK 

« Hide

References

[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. expand/collapse author list , 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]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN44513.2.
AE014073 Genomic DNA. Translation: AAP18324.1.
RefSeqNP_708806.2. NC_004337.2.
NP_838514.1. NC_004741.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF3035.

Proteomic databases

PaxDbP0AES1.
PRIDEP0AES1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN44513; AAN44513; SF3035.
AAP18324; AAP18324; S3236.
GeneID1026646.
1079490.
KEGGsfl:SF3035.
sfx:S3236.
PATRIC18708196. VBIShiFle31049_3546.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0754.
HOGENOMHOG000124980.
KOK01460.
OMAYMGYKWQ.
OrthoDBEOG66XB93.

Enzyme and pathway databases

UniPathwayUPA00204.
UPA00819.

Family and domain databases

InterProIPR007921. CHAP_dom.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view]
SUPFAMSSF52440. SSF52440. 1 hit.
PROSITEPS50911. CHAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSP_SHIFL
AccessionPrimary (citable) accession number: P0AES1
Secondary accession number(s): P43675
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 9, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways