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P0AES1

- GSP_SHIFL

UniProt

P0AES1 - GSP_SHIFL

Protein

Bifunctional glutathionylspermidine synthetase/amidase

Gene

gss

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
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    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

    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 – 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.
    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.
    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: October 1, 2014
    This is version 63 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