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P0AES1

- GSP_SHIFL

UniProt

P0AES1 - GSP_SHIFL

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Protein

Bifunctional glutathionylspermidine synthetase/amidase

Gene
gss, gsp, SF3035, S3236
Organism
Shigella flexneri
Status
Reviewed - 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.
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 – 581Gsp By similarity
Active sitei59 – 591S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediate By similarity
Binding sitei64 – 641Gsp By similarity
Sitei131 – 1311Increases nucleophilicity of active site Cys; for amidase activity By similarity
Binding sitei149 – 1491Gsp By similarity
Binding sitei316 – 3161Glutathione By similarity
Sitei316 – 3161Transition state stabilizer; for synthetase activity By similarity
Metal bindingi318 – 3181Magnesium 1 By similarity
Metal bindingi330 – 3301Magnesium 1 By similarity
Metal bindingi330 – 3301Magnesium 2 By similarity
Metal bindingi332 – 3321Magnesium 2 By similarity
Binding sitei335 – 3351Glutathione By similarity
Binding sitei391 – 3911Spermidine By similarity
Binding sitei392 – 3921Glutathione By similarity
Binding sitei446 – 4461Glutathione By similarity
Binding sitei498 – 4981ATP By similarity
Binding sitei533 – 5331ATP By similarity
Binding sitei582 – 5821ATP By similarity
Binding sitei610 – 6101Spermidine By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi316 – 3183ATP By similarity
Nucleotide bindingi539 – 5402ATP By similarity
Nucleotide bindingi568 – 5714ATP By similarity
Nucleotide bindingi603 – 6053ATP By 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
ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Cysteine sulfenic acid (-SOH); transient By 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 176143Peptidase C51Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 195194Gsp amidaseAdd
BLAST
Regioni78 – 814Gsp binding By 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.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0754.
HOGENOMiHOG000124980.
KOiK01460.
OMAiYMGYKWQ.
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

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MSKGTTSQDA PFGTLLGYAP GGVAIYSSDY SSLDPQEYED DAVFRSYIDD    50
EYMGHKWQCV EFARRFLFLN YGVVFTDVGM AWEIFSLRFL REVVNDNILP 100
LQAFPNGSPR APVAGALLIW DKGGEFKDTG HVAIITQLHG NKVRIAEQNV 150
IHSPLPQGQQ WTRELEMVVE NGCYTLKDTF DDTTILGWMI QTEDTEYSLP 200
QPEIAGELLK ISGARLENKG QFDGKWLDEK DPLQNAYVQA NGQVINQDPY 250
HYYTITESAE QELIKATNEL HLMYLHATDK VLKDDNLLAL FDIPKILWPR 300
LRLSWQRRRH HMITGRMDFC MDERGLKVYE YNADSASCHT EAGLILERWA 350
EQGYKGNGFN PAEGLINELA GAWKHSRARP FVHIMQDKDI EENYHAQFME 400
QALHQAGFET RILRGLDELG WDAAGQLIDG EGRLVNCVWK TWAWETAFDQ 450
IREVSDREFA AVPIRTGHPQ NEVRLIDVLL RPEVLVFEPL WTVIPGNKAI 500
LPILWSLFPH HRYLLDTDFT VNDELVKTGY AVKPIAGRCG SNIDLVSHHE 550
EVLDKTSGKF AEQKNIYQQL WCLPKVDGKY IQVCTFTVGG NYGGTCLRGD 600
ESLVIKKESD IEPLIVVKK 619
Length:619
Mass (Da):70,532
Last modified:December 20, 2005 - v1
Checksum:i07FB43D8A0B2933C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN44513.2 .
AE014073 Genomic DNA. Translation: AAP18324.1 .
RefSeqi NP_708806.2. NC_004337.2.
NP_838514.1. NC_004741.1.

3D structure databases

ProteinModelPortali P0AES1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198214.SF3035.

Proteomic databases

PaxDbi P0AES1.
PRIDEi P0AES1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN44513 ; AAN44513 ; SF3035 .
AAP18324 ; AAP18324 ; S3236 .
GeneIDi 1026646.
1079490.
KEGGi sfl:SF3035.
sfx:S3236.
PATRICi 18708196. VBIShiFle31049_3546.

Phylogenomic databases

eggNOGi COG0754.
HOGENOMi HOG000124980.
KOi K01460.
OMAi YMGYKWQ.
OrthoDBi EOG66XB93.

Enzyme and pathway databases

UniPathwayi UPA00204 .
UPA00819 .

Family and domain databases

InterProi IPR007921. CHAP_dom.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view ]
Pfami PF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view ]
SUPFAMi SSF52440. SSF52440. 1 hit.
PROSITEi PS50911. CHAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 62 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

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