Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q73EN1

- PUR9_BACC1

UniProt

Q73EN1 - PUR9_BACC1

Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    Ordered Locus Names:BCE_0327
    OrganismiBacillus cereus (strain ATCC 10987)
    Taxonomic identifieri222523 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000002527: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 511511Bifunctional purine biosynthesis protein PurHPRO_1000018839Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi222523.BCE_0327.

    Structurei

    3D structure databases

    ProteinModelPortaliQ73EN1.
    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.
    HOGENOMiHOG000230373.
    KOiK00602.
    OMAiGIGQADN.
    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.

    Q73EN1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKRALVSVS DKTGVVEFVK GLLEQGIEVI STGGTKKLLE ENGLQVIGIS    50
    EVTGFPEIMD GRVKTLHPNI HGGLLAVRDN ETHVAQMNEL GIEPIDFVIV 100
    NLYPFKETIA KPDVTFADAI ENIDIGGPTM IRSAAKNHKF VSVIVDPVDY 150
    DVVLAELEEN GEVKEETKRK LAAKVFRHTA AYDALISNYL TEQMGEESPE 200
    TLTVTFEKKQ DLRYGENPHQ KATFYKAPFA ATSSVAYAEQ LHGKELSYNN 250
    INDADAALSI VKEFTEPAVV AVKHMNPCGV GVGTDIHEAY TRAYEADPVS 300
    IFGGIIAANR EIDKSTAEKL HEIFLEIIIA PSFSKEALEV LQNKKNLRLL 350
    TVNIEKSTSA SKKLTSVQGG LLVQEEDTLS LDESTISIPT KREPSEQEWK 400
    DLKLAWKVVK HVKSNAIVLA KDDMTIGVGA GQMNRVGSAK IAITQAGEKA 450
    QGSALASDAF FPMPDTLEEA AKAGITAIIQ PGGSIRDEDS IKVADTYGIA 500
    MVFTGVRHFK H 511
    Length:511
    Mass (Da):55,643
    Last modified:July 5, 2004 - v1
    Checksum:iF8D8A456B4774A6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS39263.1.
    RefSeqiNP_976655.1. NC_003909.8.
    WP_000745401.1. NC_003909.8.

    Genome annotation databases

    EnsemblBacteriaiAAS39263; AAS39263; BCE_0327.
    GeneIDi2750147.
    KEGGibca:BCE_0327.
    PATRICi18849534. VBIBacCer118379_0314.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS39263.1 .
    RefSeqi NP_976655.1. NC_003909.8.
    WP_000745401.1. NC_003909.8.

    3D structure databases

    ProteinModelPortali Q73EN1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 222523.BCE_0327.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS39263 ; AAS39263 ; BCE_0327 .
    GeneIDi 2750147.
    KEGGi bca:BCE_0327.
    PATRICi 18849534. VBIBacCer118379_0314.

    Phylogenomic databases

    eggNOGi COG0138.
    HOGENOMi HOG000230373.
    KOi K00602.
    OMAi GIGQADN.
    OrthoDBi EOG6QCDFF.

    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. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
      Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
      Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10987.

    Entry informationi

    Entry nameiPUR9_BACC1
    AccessioniPrimary (citable) accession number: Q73EN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 70 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3