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P90518

- GSP_CRIFA

UniProt

P90518 - GSP_CRIFA

Protein

Glutathionylspermidine synthase

Gene

GSP

Organism
Crithidia fasciculata
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 2 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Conjugates glutathione (gamma-Glu-Cys-Gly) and spermidine to form glutathionylspermidine in the biosynthesis trypanothione (N1,N(8)-bis(glutathionyl)spermidine), which is involved in maintaining intracellular thiol redox and in defense against oxidants.

    Catalytic activityi

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

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei350 – 3501GlutathioneBy similarity
    Sitei350 – 3501Transition state stabilizerBy similarity
    Metal bindingi352 – 3521Magnesium 1By similarity
    Metal bindingi364 – 3641Magnesium 1By similarity
    Metal bindingi364 – 3641Magnesium 2By similarity
    Metal bindingi366 – 3661Magnesium 2By similarity
    Binding sitei369 – 3691GlutathioneBy similarity
    Binding sitei432 – 4321SpermidineBy similarity
    Binding sitei433 – 4331GlutathioneBy similarity
    Binding sitei501 – 5011GlutathioneBy similarity
    Binding sitei544 – 5441ATPBy similarity
    Binding sitei579 – 5791ATPBy similarity
    Binding sitei586 – 5861ATP; via amide nitrogenBy similarity
    Binding sitei653 – 6531ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi350 – 3523ATPBy similarity
    Nucleotide bindingi689 – 6913ATPBy similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi6.3.1.8. 1365.
    SABIO-RKP90518.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathionylspermidine synthase (EC:6.3.1.8)
    Gene namesi
    Name:GSP
    OrganismiCrithidia fasciculata
    Taxonomic identifieri5656 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 719719Glutathionylspermidine synthasePRO_0000070442Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Interactioni

    Structurei

    3D structure databases

    ProteinModelPortaliP90518.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 200147Peptidase C51PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    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.

    P90518-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSLPHNHHY ETHHRGTAEV PFDELIGVTP DGVPVISNGN EAHFSNLESI    50
    TAACLPLSSF ERKAPCKQPY RKMGVKWQCV EFVRRYLASR KAVWMTSLCT 100
    AEEVWREENL FVDVRDGRPV EVVRTPNKST GPAPAVADIV VWGEGPETPF 150
    GHVAIVTEVC ASCVRVAEQN QGFEKWPEDV PFSREIAMRT TESGEVELLD 200
    EDPLLGWVTV QAPFYNFDDG DLADSFRLVV GQGQILRQPF PKHVDVPWLN 250
    TGEECDTILK HSLVVDGNMG EGAHAEEGDV PGAFYFLDYD MFCRLGRAAS 300
    SLHRIAMAAT AKVLEDPEST HLLEHYFGVP PEIQPLLRRS WEMTPPMGGR 350
    FDFGYDGKNV VMLEYNCDSS GALLECCNTQ EKMARFYGVS QGTSTGSFLG 400
    AKCVTYFQRL LTNEKVCPQH RLIHFMIDED DEERYTARCM MGFAEQAGFR 450
    TKLCVKLVNF RYRDGPPSNA APLATPCDHP TIVDGEDEEV LMVWKTWSWD 500
    TVLHQYHSQR SSSDAVNTPT LSDILLNNNI RVLEPLWKAV TGSKAILPFM 550
    HALAPDHEHM LAASFLPTRE IISRHYISKP VNGRAGQNIM MYDPVTSPTE 600
    LEGAPQQDIC EALSQNASAR SLLNGSPLPL SQSVDQTNEC SPGKFFDSVL 650
    VYQQRLFLKK FDGKYFPIFC GWMVGDEFGG VVVREDTSKI TKLSSMVVPA 700
    RVVRDNVPLG VSYSDEGET 719
    Length:719
    Mass (Da):80,322
    Last modified:March 1, 2001 - v2
    Checksum:i46069BE9C40EEEFC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66520 Genomic DNA. Translation: AAC48361.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66520 Genomic DNA. Translation: AAC48361.2 .

    3D structure databases

    ProteinModelPortali P90518.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P90518.
    ChEMBLi CHEMBL3354.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 6.3.1.8. 1365.
    SABIO-RK P90518.

    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. "Cloning and characterization of the two enzymes responsible for trypanothione biosynthesis in Crithidia fasciculata."
      Tetaud E., Manai F., Barrett M.P., Nadeau K., Walsh C.T., Fairlamb A.H.
      J. Biol. Chem. 273:19383-19390(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: HS6.
    2. "Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata."
      Smith K., Nadeau K., Bradley M., Walsh C., Fairlamb A.H.
      Protein Sci. 1:874-883(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 191-209; 351-358; 512-530; 532-538 AND 695-710, CHARACTERIZATION.

    Entry informationi

    Entry nameiGSP_CRIFA
    AccessioniPrimary (citable) accession number: P90518
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 60 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3