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Protein

N5-carboxyaminoimidazole ribonucleotide mutase

Gene

purE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).UniRule annotation1 Publication

Caution

Was originally thought to be the catalytic subunit of phosphoribosylaminoimidazole carboxylase, with ATPase subunit PurK.1 Publication

Catalytic activityi

5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.UniRule annotation2 Publications

Kineticsi

  1. KM=140 µM for N5-CAIR1 Publication

    Pathwayi: IMP biosynthesis via de novo pathway

    This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route).UniRule annotation1 Publication
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. N5-carboxyaminoimidazole ribonucleotide synthase (purK)
    2. N5-carboxyaminoimidazole ribonucleotide mutase (purE)
    This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei16SubstrateUniRule annotation1 Publication1
    Binding sitei19SubstrateUniRule annotation1 Publication1
    Binding sitei46SubstrateUniRule annotation1 Publication1

    GO - Molecular functioni

    • 5-(carboxyamino)imidazole ribonucleotide mutase activity Source: EcoCyc
    • identical protein binding Source: IntAct

    GO - Biological processi

    Keywordsi

    Molecular functionIsomerase
    Biological processPurine biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:PURE-MONOMER
    MetaCyc:PURE-MONOMER
    BRENDAi5.4.99.18 2026
    UniPathwayiUPA00074; UER00943

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N5-carboxyaminoimidazole ribonucleotide mutaseUniRule annotationCurated (EC:5.4.99.18UniRule annotation2 Publications)
    Short name:
    N5-CAIR mutaseUniRule annotationCurated
    Alternative name(s):
    5-(carboxyamino)imidazole ribonucleotide mutaseUniRule annotationCurated
    Gene namesi
    Name:purEUniRule annotation
    Ordered Locus Names:b0523, JW0512
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10793 purE

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000749732 – 169N5-carboxyaminoimidazole ribonucleotide mutaseAdd BLAST168

    Proteomic databases

    PaxDbiP0AG18
    PRIDEiP0AG18

    2D gel databases

    SWISS-2DPAGEiP0AG18

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-909394,EBI-909394

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi4261243, 17 interactors
    DIPiDIP-10610N
    IntActiP0AG18, 11 interactors
    STRINGi316385.ECDH10B_0479

    Structurei

    Secondary structure

    1169
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi10 – 16Combined sources7
    Helixi17 – 19Combined sources3
    Helixi20 – 33Combined sources14
    Beta strandi37 – 41Combined sources5
    Turni44 – 46Combined sources3
    Helixi48 – 57Combined sources10
    Turni58 – 62Combined sources5
    Beta strandi64 – 70Combined sources7
    Helixi76 – 82Combined sources7
    Beta strandi88 – 92Combined sources5
    Turni96 – 100Combined sources5
    Helixi101 – 108Combined sources8
    Helixi123 – 138Combined sources16
    Helixi142 – 160Combined sources19

    3D structure databases

    ProteinModelPortaliP0AG18
    SMRiP0AG18
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AG18

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AIR carboxylase family. Class I subfamily.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4108UM6 Bacteria
    COG0041 LUCA
    HOGENOMiHOG000034140
    InParanoidiP0AG18
    KOiK01588
    OMAiSNSIDGW
    PhylomeDBiP0AG18

    Family and domain databases

    Gene3Di3.40.50.7700, 1 hit
    HAMAPiMF_01929 PurE_classI, 1 hit
    InterProiView protein in InterPro
    IPR033747 PurE_ClassI
    IPR000031 PurE_dom
    IPR024694 PurE_prokaryotes
    IPR035893 PurE_sf
    PfamiView protein in Pfam
    PF00731 AIRC, 1 hit
    PIRSFiPIRSF001338 AIR_carboxylase, 1 hit
    SMARTiView protein in SMART
    SM01001 AIRC, 1 hit
    SUPFAMiSSF52255 SSF52255, 1 hit
    TIGRFAMsiTIGR01162 purE, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AG18-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSRNNPARV AIVMGSKSDW ATMQFAAEIF EILNVPHHVE VVSAHRTPDK
    60 70 80 90 100
    LFSFAESAEE NGYQVIIAGA GGAAHLPGMI AAKTLVPVLG VPVQSAALSG
    110 120 130 140 150
    VDSLYSIVQM PRGIPVGTLA IGKAGAANAA LLAAQILATH DKELHQRLND
    160
    WRKAQTDEVL ENPDPRGAA
    Length:169
    Mass (Da):17,780
    Last modified:January 23, 2007 - v2
    Checksum:iE8B745B8D86E7D0B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X12982 Genomic DNA Translation: CAA31420.1
    M19657 Genomic DNA Translation: AAA24449.1
    U82664 Genomic DNA Translation: AAB40276.1
    U00096 Genomic DNA Translation: AAC73625.1
    AP009048 Genomic DNA Translation: BAE76300.1
    PIRiJT0499 DEECPE
    RefSeqiNP_415056.1, NC_000913.3
    WP_001295318.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC73625; AAC73625; b0523
    BAE76300; BAE76300; BAE76300
    GeneIDi949031
    KEGGiecj:JW0512
    eco:b0523
    PATRICifig|1411691.4.peg.1755

    Similar proteinsi

    Entry informationi

    Entry nameiPURE_ECOLI
    AccessioniPrimary (citable) accession number: P0AG18
    Secondary accession number(s): P09028, Q2MBQ6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 23, 2007
    Last modified: March 28, 2018
    This is version 103 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

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