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P15639

- PUR9_ECOLI

UniProt

P15639 - PUR9_ECOLI

Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      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.
    IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

    Pathwayi

    GO - Molecular functioni

    1. IMP cyclohydrolase activity Source: EcoCyc
    2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: EcoCyc

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
    2. biofilm formation Source: CACAO

    Keywords - Molecular functioni

    Hydrolase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:AICARTRANSIMPCYCLO-CPLX.
    ECOL316407:JW3970-MONOMER.
    MetaCyc:AICARTRANSIMPCYCLO-CPLX.
    UniPathwayiUPA00074; UER00133.
    UPA00074; UER00135.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional purine biosynthesis protein PurH
    Including the following 2 domains:
    Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
    Alternative name(s):
    AICAR transformylase
    IMP cyclohydrolase (EC:3.5.4.10)
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
    Gene namesi
    Name:purH
    Ordered Locus Names:b4006, JW3970
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10795. purH.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Bifunctional purine biosynthesis protein PurHPRO_0000192091Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei287 – 2871N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP15639.
    PRIDEiP15639.

    2D gel databases

    SWISS-2DPAGEP15639.

    Expressioni

    Gene expression databases

    GenevestigatoriP15639.

    Interactioni

    Protein-protein interaction databases

    IntActiP15639. 7 interactions.
    STRINGi511145.b4006.

    Structurei

    3D structure databases

    ProteinModelPortaliP15639.
    SMRiP15639. Positions 4-529.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The IMP cyclohydrolase activity resides in the N-terminal region.By similarity

    Sequence similaritiesi

    Belongs to the PurH family.Curated

    Phylogenomic databases

    eggNOGiCOG0138.
    HOGENOMiHOG000230372.
    KOiK00602.
    OMAiRAFKTDP.
    OrthoDBiEOG6QCDFF.
    PhylomeDBiP15639.

    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.

    P15639-1 [UniParc]FASTAAdd to Basket

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    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 IKKLDMRYGE NSHQQAAFYI EENVKEASVA 250
    TATQVQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PCGVAIGNSI 300
    LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSASE 350
    EALKITAAKQ NVRVLTCGQW GERVPGLDFK RVNGGLLVQD RDLGMVGAEE 400
    LRVVTKRQPS EQELRDALFC WKVAKFVKSN AIVYAKNNMT IGIGAGQMSR 450
    VYSAKIAGIK AADEGLEVKG SSMASDAFFP FRDGIDAAAA AGVTCVIQPG 500
    GSIRDDEVIA AADEHGIAML FTDMRHFRH 529
    Length:529
    Mass (Da):57,329
    Last modified:April 1, 1990 - v1
    Checksum:iDC034ED01915DA68
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05126 Genomic DNA. Translation: AAA24454.1.
    X51950 Genomic DNA. Translation: CAA36212.1.
    U00006 Genomic DNA. Translation: AAC43104.1.
    U00096 Genomic DNA. Translation: AAC76980.1.
    AP009048 Genomic DNA. Translation: BAE77313.1.
    PIRiB34193. DTECPH.
    RefSeqiNP_418434.1. NC_000913.3.
    YP_491454.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76980; AAC76980; b4006.
    BAE77313; BAE77313; BAE77313.
    GeneIDi12933467.
    948503.
    KEGGiecj:Y75_p3190.
    eco:b4006.
    PATRICi32123537. VBIEscCol129921_4121.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05126 Genomic DNA. Translation: AAA24454.1 .
    X51950 Genomic DNA. Translation: CAA36212.1 .
    U00006 Genomic DNA. Translation: AAC43104.1 .
    U00096 Genomic DNA. Translation: AAC76980.1 .
    AP009048 Genomic DNA. Translation: BAE77313.1 .
    PIRi B34193. DTECPH.
    RefSeqi NP_418434.1. NC_000913.3.
    YP_491454.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P15639.
    SMRi P15639. Positions 4-529.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P15639. 7 interactions.
    STRINGi 511145.b4006.

    2D gel databases

    SWISS-2DPAGE P15639.

    Proteomic databases

    PaxDbi P15639.
    PRIDEi P15639.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76980 ; AAC76980 ; b4006 .
    BAE77313 ; BAE77313 ; BAE77313 .
    GeneIDi 12933467.
    948503.
    KEGGi ecj:Y75_p3190.
    eco:b4006.
    PATRICi 32123537. VBIEscCol129921_4121.

    Organism-specific databases

    EchoBASEi EB0788.
    EcoGenei EG10795. purH.

    Phylogenomic databases

    eggNOGi COG0138.
    HOGENOMi HOG000230372.
    KOi K00602.
    OMAi RAFKTDP.
    OrthoDBi EOG6QCDFF.
    PhylomeDBi P15639.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00133 .
    UPA00074 ; UER00135 .
    BioCyci EcoCyc:AICARTRANSIMPCYCLO-CPLX.
    ECOL316407:JW3970-MONOMER.
    MetaCyc:AICARTRANSIMPCYCLO-CPLX.

    Miscellaneous databases

    PROi P15639.

    Gene expression databases

    Genevestigatori P15639.

    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. "Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli."
      Aiba A., Mizobuchi K.
      J. Biol. Chem. 264:21239-21246(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Purine biosynthesis in Escherichia coli K12: structure and DNA sequence studies of the purHD locus."
      Flannigan K.A., Hennigan S.H., Vogelbacker H.H., Gots J.S., Smith J.M.
      Mol. Microbiol. 4:381-392(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    7. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiPUR9_ECOLI
    AccessioniPrimary (citable) accession number: P15639
    Secondary accession number(s): Q2M8U3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 124 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, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3