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Q8X611

- PUR9_ECO57

UniProt

Q8X611 - PUR9_ECO57

Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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

    BioCyciECOL386585:GJFA-4929-MONOMER.
    ECOO157:PURH-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:Z5583, ECs4929
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Bifunctional purine biosynthesis protein PurHPRO_0000192093Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei287 – 2871N6-acetyllysineUniRule annotation

    Keywords - PTMi

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi155864.Z5583.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8X611.
    SMRiQ8X611. Positions 8-529.
    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.
    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.

    Q8X611-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQQRRPVRRA LLSVSDKAGI VEFAQALSAR GVELLSTGGT ARLLAEKGLP    50
    VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EEHQIQPIDM 100
    VVVNLYPFAQ TVAREGCSLE DAVENIDIGG PTMVRSAAKN HKDVAIVVKS 150
    SDYDAIIKEM DDNEGSLTLA TRFDLAIKAF EHTAAYDSMI ANYFGSMVPA 200
    YHGESKEAAG RFPRTLNLNF IKKQDMRYGE NSHQQAAFYI EENVKEASVA 250
    TATQVQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PCGVAIGNSI 300
    LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSASE 350
    EALKITAAKQ NVRVLTCGQW GERVPGLDFK RVNGGLLVQD RDLGMVGAEE 400
    LRVVTKRQPT EQELRDALFC WKVAKFVKSN AIVYAKNNMT IGIGAGQMSR 450
    VYSAKIAGIK AADEGLEVKG SSMASDAFFP FRDGIDAAAA AGVTCVIQPG 500
    GSIRDDEVIA AADEHGIAML FTDMRHFRH 529
    Length:529
    Mass (Da):57,358
    Last modified:March 1, 2002 - v1
    Checksum:iF0FDD9FB71CAB1B1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG59203.1.
    BA000007 Genomic DNA. Translation: BAB38352.1.
    PIRiA98245.
    G86092.
    RefSeqiNP_290638.1. NC_002655.2.
    NP_312956.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG59203; AAG59203; Z5583.
    BAB38352; BAB38352; BAB38352.
    GeneIDi914853.
    960123.
    KEGGiece:Z5583.
    ecs:ECs4929.
    PATRICi18359553. VBIEscCol44059_4917.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG59203.1 .
    BA000007 Genomic DNA. Translation: BAB38352.1 .
    PIRi A98245.
    G86092.
    RefSeqi NP_290638.1. NC_002655.2.
    NP_312956.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali Q8X611.
    SMRi Q8X611. Positions 8-529.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z5583.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG59203 ; AAG59203 ; Z5583 .
    BAB38352 ; BAB38352 ; BAB38352 .
    GeneIDi 914853.
    960123.
    KEGGi ece:Z5583.
    ecs:ECs4929.
    PATRICi 18359553. VBIEscCol44059_4917.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00133 .
    UPA00074 ; UER00135 .
    BioCyci ECOL386585:GJFA-4929-MONOMER.
    ECOO157:PURH-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiPUR9_ECO57
    AccessioniPrimary (citable) accession number: Q8X611
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 28, 2003
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 79 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