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)

Q0I557

- PUR9_HISS1

UniProt

Q0I557 - PUR9_HISS1

Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Histophilus somni (strain 129Pt) (Haemophilus somnus)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (03 Oct 2006)
      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

    BioCyciHSOM205914:GJ7V-1706-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:HS_1625
    OrganismiHistophilus somni (strain 129Pt) (Haemophilus somnus)
    Taxonomic identifieri205914 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
    ProteomesiUP000001970: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 532532Bifunctional purine biosynthesis protein PurHPRO_1000018892Add
    BLAST

    Proteomic databases

    PRIDEiQ0I557.

    Interactioni

    Protein-protein interaction databases

    STRINGi205914.HS_1625.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0I557.
    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.
    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.

    Q0I557-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLNHPIRQA LLSVSDKSGI VEFAQGLVKR GVKLLSTGGT AKLLAENGIP    50
    VTEVSDYTGF PEMMEGRVKT LHPKIHGGIL GRRGIDDEVM MQHQIDAIDM 100
    VVVNLYPFAA TVAKPDCTLE DAVENIDIGG PTMVRSAAKN HQHVAIVVNN 150
    SDFNAILAEM DQNRNSLTLE TRFDLAIKAF EHTAQYDSMI ANYFGQMVKP 200
    YFRAEEEAEA KCGQFPRTLN LNFIRKQSMR YGENGHQKAA FYVEQDVKEA 250
    SVSTAKQLQG KALSYNNIAD TDAALECVKS FSEPACVIVK HANPCGVALG 300
    KDILEAYNRA YQTDPTSAFG GIIAFNRELD EDTAKAIIER QFVEVIIAPT 350
    VSSAAQEIVK SKKNVRLLTC GNWESAIQRL DFKRVNGGLL VQEADLSMVD 400
    LADLEVVSKR QPTKQELEDL LFCWKVAKFV KSNAIVYAKN NQTVGIGAGQ 450
    MSRVYSAKIA GIKAKDEGLE VKGCVMASDA FFPFRDGIDA AAKVGIECVI 500
    HPGGSMRDQE VIDAANEHNM VMVLTKMRHF RH 532
    Length:532
    Mass (Da):58,521
    Last modified:October 3, 2006 - v1
    Checksum:iB4B1BE8963C9161C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000436 Genomic DNA. Translation: ABI25893.1.
    RefSeqiWP_011609771.1. NC_008309.1.
    YP_719830.1. NC_008309.1.

    Genome annotation databases

    EnsemblBacteriaiABI25893; ABI25893; HS_1625.
    GeneIDi4241152.
    KEGGihso:HS_1625.
    PATRICi20283407. VBIHaeSom53361_1703.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000436 Genomic DNA. Translation: ABI25893.1 .
    RefSeqi WP_011609771.1. NC_008309.1.
    YP_719830.1. NC_008309.1.

    3D structure databases

    ProteinModelPortali Q0I557.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 205914.HS_1625.

    Proteomic databases

    PRIDEi Q0I557.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABI25893 ; ABI25893 ; HS_1625 .
    GeneIDi 4241152.
    KEGGi hso:HS_1625.
    PATRICi 20283407. VBIHaeSom53361_1703.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00133 .
    UPA00074 ; UER00135 .
    BioCyci HSOM205914:GJ7V-1706-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. "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
      Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
      J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 129Pt.

    Entry informationi

    Entry nameiPUR9_HISS1
    AccessioniPrimary (citable) accession number: Q0I557
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 61 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