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B5YLE5

- PUR9_THEYD

UniProt

B5YLE5 - PUR9_THEYD

Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (25 Nov 2008)
      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

    BioCyciTYEL289376:GH9L-1236-MONOMER.
    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
    Ordered Locus Names:THEYE_A1243
    OrganismiThermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
    Taxonomic identifieri289376 [NCBI]
    Taxonomic lineageiBacteriaNitrospiraeNitrospiralesNitrospiraceaeThermodesulfovibrio
    ProteomesiUP000000718: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 522522Bifunctional purine biosynthesis protein PurHPRO_1000096105Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi289376.THEYE_A1243.

    Structurei

    3D structure databases

    ProteinModelPortaliB5YLE5.
    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

    Phylogenomic databases

    eggNOGiCOG0138.
    HOGENOMiHOG000230372.
    KOiK00602.
    OMAiHRRAHAC.
    OrthoDBiEOG6QCDFF.

    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.

    B5YLE5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIKRALISVS DKRGLVDFAK ELDKLGVEIL STGGTAKTLR DSGIKVIDVS    50
    QYTGFPEIMD GRVKTLHPLI HGGILARRDN KEDIEAMERL GIKPIDMVVV 100
    NLYPFESVAK KHLSQILQPS DLNLQAFLEE AIENIDIGGP TLLRASAKNY 150
    KDVIVIVDPD DYSSIIEDIK KGSVSIEKKF ELAKKVFSHT ARYDALIADY 200
    FEKISPSGFK KDWTLPLKMT RTLRYGENPH QKAALYALNE SPSLIDADVL 250
    QGKEMSFNNY LDTHSAVLLA TEFSEPVCVI VKHNNPCGVA IGENIHTAYK 300
    KAFECDPVSA FGGIIAFNRV VDKETASEII NTFYEVIVAP DFDKDALEVF 350
    ETKKNLRLLR FPSLSDKIQP SGFDLKRILG GFIVQEWDKV DNEFSQAKVV 400
    TKRQPTDEEW KALKFAWKVC KHIKSNAVVY AKEDRTVGLG IGQTSRVFSA 450
    KIGAMHALSS LKGTVVASDG FFPFRDNIDV LAQNGVTSII QPGGSVRDQE 500
    VIDAANQYNI AMVFTGIRHF RH 522
    Length:522
    Mass (Da):58,100
    Last modified:November 25, 2008 - v1
    Checksum:i83323A65C8570910
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001147 Genomic DNA. Translation: ACI21021.1.
    RefSeqiYP_002249060.1. NC_011296.1.

    Genome annotation databases

    EnsemblBacteriaiACI21021; ACI21021; THEYE_A1243.
    GeneIDi6943286.
    KEGGitye:THEYE_A1243.
    PATRICi23909503. VBITheYel104483_1215.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001147 Genomic DNA. Translation: ACI21021.1 .
    RefSeqi YP_002249060.1. NC_011296.1.

    3D structure databases

    ProteinModelPortali B5YLE5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 289376.THEYE_A1243.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACI21021 ; ACI21021 ; THEYE_A1243 .
    GeneIDi 6943286.
    KEGGi tye:THEYE_A1243.
    PATRICi 23909503. VBITheYel104483_1215.

    Phylogenomic databases

    eggNOGi COG0138.
    HOGENOMi HOG000230372.
    KOi K00602.
    OMAi HRRAHAC.
    OrthoDBi EOG6QCDFF.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00133 .
    UPA00074 ; UER00135 .
    BioCyci TYEL289376:GH9L-1236-MONOMER.

    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. "The complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87."
      Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51303 / DSM 11347 / YP87.

    Entry informationi

    Entry nameiPUR9_THEYD
    AccessioniPrimary (citable) accession number: B5YLE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 45 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, Reference proteome

    Documents

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

    External Data

    Dasty 3