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Protein

N5-carboxyaminoimidazole ribonucleotide mutase

Gene

purE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei16 – 161SubstrateUniRule annotation1 Publication
    Binding sitei19 – 191SubstrateUniRule annotation1 Publication
    Binding sitei46 – 461SubstrateUniRule annotation1 Publication

    GO - Molecular functioni

    • 5-(carboxyamino)imidazole ribonucleotide mutase activity Source: EcoCyc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:PURE-MONOMER.
    ECOL316407:JW0512-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10793. purE.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 169168N5-carboxyaminoimidazole ribonucleotide mutasePRO_0000074973Add
    BLAST

    Proteomic databases

    PaxDbiP0AG18.
    PRIDEiP0AG18.

    2D gel databases

    SWISS-2DPAGEP0AG18.

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Protein-protein interaction databases

    BioGridi4261243. 17 interactions.
    DIPiDIP-10610N.
    IntActiP0AG18. 11 interactions.
    STRINGi511145.b0523.

    Structurei

    Secondary structure

    1
    169
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 167Combined sources
    Helixi17 – 193Combined sources
    Helixi20 – 3314Combined sources
    Beta strandi37 – 415Combined sources
    Turni44 – 463Combined sources
    Helixi48 – 5710Combined sources
    Turni58 – 625Combined sources
    Beta strandi64 – 707Combined sources
    Helixi76 – 827Combined sources
    Beta strandi88 – 925Combined sources
    Turni96 – 1005Combined sources
    Helixi101 – 1088Combined sources
    Helixi123 – 13816Combined sources
    Helixi142 – 16019Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D7AX-ray2.50A/B/C/D/L/M/N/O8-167[»]
    1QCZX-ray1.50A1-169[»]
    2ATEX-ray1.80A1-169[»]
    2NSHX-ray1.80A1-169[»]
    2NSJX-ray2.31A1-169[»]
    2NSLX-ray2.00A1-169[»]
    ProteinModelPortaliP0AG18.
    SMRiP0AG18. Positions 7-168.
    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.
    OMAiSDWATMR.
    PhylomeDBiP0AG18.

    Family and domain databases

    Gene3Di3.40.50.7700. 1 hit.
    HAMAPiMF_01929. PurE_classI. 1 hit.
    InterProiIPR000031. PurE_dom.
    IPR024694. PurE_prokaryotes.
    [Graphical view]
    PfamiPF00731. AIRC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001338. AIR_carboxylase. 1 hit.
    SMARTiSM01001. AIRC. 1 hit.
    [Graphical view]
    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.
    PATRICi32116206. VBIEscCol129921_0544.

    Cross-referencesi

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D7AX-ray2.50A/B/C/D/L/M/N/O8-167[»]
    1QCZX-ray1.50A1-169[»]
    2ATEX-ray1.80A1-169[»]
    2NSHX-ray1.80A1-169[»]
    2NSJX-ray2.31A1-169[»]
    2NSLX-ray2.00A1-169[»]
    ProteinModelPortaliP0AG18.
    SMRiP0AG18. Positions 7-168.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261243. 17 interactions.
    DIPiDIP-10610N.
    IntActiP0AG18. 11 interactions.
    STRINGi511145.b0523.

    2D gel databases

    SWISS-2DPAGEP0AG18.

    Proteomic databases

    PaxDbiP0AG18.
    PRIDEiP0AG18.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73625; AAC73625; b0523.
    BAE76300; BAE76300; BAE76300.
    GeneIDi949031.
    KEGGiecj:JW0512.
    eco:b0523.
    PATRICi32116206. VBIEscCol129921_0544.

    Organism-specific databases

    EchoBASEiEB0786.
    EcoGeneiEG10793. purE.

    Phylogenomic databases

    eggNOGiENOG4108UM6. Bacteria.
    COG0041. LUCA.
    HOGENOMiHOG000034140.
    InParanoidiP0AG18.
    KOiK01588.
    OMAiSDWATMR.
    PhylomeDBiP0AG18.

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00943.
    BioCyciEcoCyc:PURE-MONOMER.
    ECOL316407:JW0512-MONOMER.
    MetaCyc:PURE-MONOMER.
    BRENDAi5.4.99.18. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0AG18.
    PROiP0AG18.

    Family and domain databases

    Gene3Di3.40.50.7700. 1 hit.
    HAMAPiMF_01929. PurE_classI. 1 hit.
    InterProiIPR000031. PurE_dom.
    IPR024694. PurE_prokaryotes.
    [Graphical view]
    PfamiPF00731. AIRC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001338. AIR_carboxylase. 1 hit.
    SMARTiSM01001. AIRC. 1 hit.
    [Graphical view]
    SUPFAMiSSF52255. SSF52255. 1 hit.
    TIGRFAMsiTIGR01162. purE. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPURE_ECOLI
    AccessioniPrimary (citable) accession number: P0AG18
    Secondary accession number(s): P09028, Q2MBQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 23, 2007
    Last modified: September 7, 2016
    This is version 92 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

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

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.