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)

A4VPK9

- PUR9_PSEU5

UniProt

A4VPK9 - PUR9_PSEU5

Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Pseudomonas stutzeri (strain A1501)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (29 May 2007)
      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

    BioCyciPSTU379731:GJER-3274-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:PST_3279
    OrganismiPseudomonas stutzeri (strain A1501)
    Taxonomic identifieri379731 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000000233: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 534534Bifunctional purine biosynthesis protein PurHPRO_1000018942Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi379731.PST_3279.

    Structurei

    3D structure databases

    ProteinModelPortaliA4VPK9.
    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.
    OMAiRAFKTDP.
    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.

    A4VPK9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDQTTRLPV RRALISVSDK TGVVDFAREL EALGVEILST GGTFKLLREN    50
    GIAAIEVADY TGFPEMMDGR VKTLHPKIHG GILGRRDLDG AVMAEHGIAP 100
    IDLVAVNLYP FAATVAKPGC TLPDAIENID IGGPTMVRSA AKNHKDVAIV 150
    VNAEDYAAVV DNLKNGGLTY AQRFDLALKA FEHTAGYDGM IANYLGGIDQ 200
    STEQLSTDNR SLFPRTYNMQ FIKAQDMRYG ENPHQQAAFY VEKPDEACVA 250
    TARQLQGKEL SFNNVADTDA ALECVKSFTK PACVIVKHAN PCGVAVVPEN 300
    EGGIRKAYDL AYATDSESAF GGIIAFNREL DGETAQAIVE RQFVEVIIAP 350
    KVSQAARDVV ASKANVRLLE CGEWPAERSP GWDYKRVNGG LLIQSRDIGM 400
    ITEADLKIVT QRAPTEQEIH DLIFAWKVAK FVKSNAIVYA KNRQTVGVGA 450
    GQMSRVNSAR IAAIKAEHAG LQVQGAVMAS DAFFPFRDGI DNAAKAGITA 500
    VIQPGGSMRD NEVIAAADEA GIAMVFTGMR HFRH 534
    Length:534
    Mass (Da):57,627
    Last modified:May 29, 2007 - v1
    Checksum:i3ACEFAC66D086BD1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000304 Genomic DNA. Translation: ABP80910.1.
    RefSeqiYP_001173752.1. NC_009434.1.

    Genome annotation databases

    EnsemblBacteriaiABP80910; ABP80910; PST_3279.
    GeneIDi5096240.
    KEGGipsa:PST_3279.
    PATRICi19967114. VBIPseStu31643_3294.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000304 Genomic DNA. Translation: ABP80910.1 .
    RefSeqi YP_001173752.1. NC_009434.1.

    3D structure databases

    ProteinModelPortali A4VPK9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 379731.PST_3279.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP80910 ; ABP80910 ; PST_3279 .
    GeneIDi 5096240.
    KEGGi psa:PST_3279.
    PATRICi 19967114. VBIPseStu31643_3294.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00133 .
    UPA00074 ; UER00135 .
    BioCyci PSTU379731:GJER-3274-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 the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."
      Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y.
      , Elmerich C., Lin M., Jin Q.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: A1501.

    Entry informationi

    Entry nameiPUR9_PSEU5
    AccessioniPrimary (citable) accession number: A4VPK9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 49 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