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Q9F1T4

- PUR9_STRSU

UniProt

Q9F1T4 - PUR9_STRSU

Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Streptococcus suis
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
    IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

    Pathwayi

    GO - Molecular functioni

    1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
    2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00133.
    UPA00074; UER00135.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional purine biosynthesis protein PurHUniRule annotation
    Including the following 2 domains:
    Phosphoribosylaminoimidazolecarboxamide formyltransferaseUniRule annotation (EC:2.1.2.3UniRule annotation)
    Alternative name(s):
    AICAR transformylaseUniRule annotation
    IMP cyclohydrolaseUniRule annotation (EC:3.5.4.10UniRule annotation)
    Alternative name(s):
    ATICUniRule annotation
    IMP synthaseUniRule annotation
    InosinicaseUniRule annotation
    Gene namesi
    Name:purHUniRule annotation
    OrganismiStreptococcus suis
    Taxonomic identifieri1307 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 515515Bifunctional purine biosynthesis protein PurHPRO_0000192139Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ9F1T4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The IMP cyclohydrolase activity resides in the N-terminal region.UniRule annotation

    Sequence similaritiesi

    Belongs to the PurH family.UniRule annotation

    Family and domain databases

    Gene3Di3.40.140.20. 2 hits.
    3.40.50.1380. 1 hit.
    HAMAPiMF_00139. PurH.
    InterProiIPR024051. AICAR_Tfase_dom.
    IPR002695. AICARFT_IMPCHas.
    IPR016193. Cytidine_deaminase-like.
    IPR011607. MGS-like_dom.
    [Graphical view]
    PANTHERiPTHR11692. PTHR11692. 1 hit.
    PfamiPF01808. AICARFT_IMPCHas. 1 hit.
    PF02142. MGS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
    SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
    SM00851. MGS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52335. SSF52335. 1 hit.
    SSF53927. SSF53927. 1 hit.
    TIGRFAMsiTIGR00355. purH. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9F1T4-1 [UniParc]FASTAAdd to Basket

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    MTKRALISVS DKNGIVEFAQ ELTKFGWEII STGGTKVALD QAGVTTIAID    50
    DVTGFPEMMD GRVKTLHPKI HGGLLARRDL DSHLQAANDH EIGLIDLVVV 100
    NLYPFKETIL RPDVTYDLAV ENIDIGGPSM LRSAAKNHAS VTVVVDPADY 150
    PTVLGEIAEQ GETSYATRQR LAAKVFRHTA AYDALIADYF TKQVGEDKPE 200
    KLTITYDLNQ PMRYGENPQQ NADFYQNALP TAYSIAAAKQ LNGKELSFNN 250
    IRDADAAIRI IRDFKDRPTV VALKHMNPCG IGQAETIEQA WDYAYEADPV 300
    SIFGGIVVLN REVDAATAEK MHPIFLEIII APGYSAEALA ILTNKKKNLR 350
    ILELAFDAQD ASEVEKEFTG VVGGLLVQDQ DVVVESPVDW QVVTERQPSE 400
    QEWAAMEFAW KSSKYVKSNG IIITNDKMTL GVGPGQTNRV ASVRIAIEQA 450
    KDRLEGAVLA SDAFFPFADN VEEIAAAGIK AIIQPGGSVR DQDSIDMANK 500
    YGLTMVFTGV RHFRH 515
    Length:515
    Mass (Da):56,511
    Last modified:March 1, 2001 - v1
    Checksum:i92D3B3B63F39288A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB045609 Genomic DNA. Translation: BAB20827.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB045609 Genomic DNA. Translation: BAB20827.1 .

    3D structure databases

    ProteinModelPortali Q9F1T4.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00133 .
    UPA00074 ; UER00135 .

    Family and domain databases

    Gene3Di 3.40.140.20. 2 hits.
    3.40.50.1380. 1 hit.
    HAMAPi MF_00139. PurH.
    InterProi IPR024051. AICAR_Tfase_dom.
    IPR002695. AICARFT_IMPCHas.
    IPR016193. Cytidine_deaminase-like.
    IPR011607. MGS-like_dom.
    [Graphical view ]
    PANTHERi PTHR11692. PTHR11692. 1 hit.
    Pfami PF01808. AICARFT_IMPCHas. 1 hit.
    PF02142. MGS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
    SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
    SM00851. MGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52335. SSF52335. 1 hit.
    SSF53927. SSF53927. 1 hit.
    TIGRFAMsi TIGR00355. purH. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Evidence for horizontal transfer of the SsuDAT1I restriction-modification genes to the Streptococcus suis genome."
      Sekizaki T., Otani Y., Osaki M., Takamatsu D., Shimoji Y.
      J. Bacteriol. 183:500-511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DAT1 / Serotype 2.

    Entry informationi

    Entry nameiPUR9_STRSU
    AccessioniPrimary (citable) accession number: Q9F1T4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 59 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

    Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3