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Protein

Xanthine phosphoribosyltransferase

Gene

gpt

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts on guanine, xanthine and to a lesser extent hypoxanthine.1 Publication

Catalytic activityi

XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Enzyme regulationi

Inhibited by thioguanine, GMP and, to a lesser extent, by thioxanthine, azaxanthine and azaguanine.1 Publication

Kineticsi

  1. KM=4.3 µM for guanine2 Publications
  2. KM=30.5 µM for xanthine2 Publications
  3. KM=90.8 µM for hypoxanthine2 Publications

    Pathway:iXMP biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes XMP from xanthine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Xanthine phosphoribosyltransferase (gpt)
    This subpathway is part of the pathway XMP biosynthesis via salvage 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 XMP from xanthine, the pathway XMP biosynthesis via salvage pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei69 – 6915-phosphoribose 1-diphosphate
    Metal bindingi89 – 891Magnesium1 Publication
    Binding sitei92 – 921Xanthine
    Binding sitei135 – 1351Xanthine; via amide nitrogen and carbonyl oxygen

    GO - Molecular functioni

    • hypoxanthine phosphoribosyltransferase activity Source: EcoCyc
    • magnesium ion binding Source: UniProtKB-HAMAP
    • xanthine phosphoribosyltransferase activity Source: EcoCyc

    GO - Biological processi

    • GMP salvage Source: EcoCyc
    • IMP salvage Source: EcoCyc
    • XMP salvage Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:GPT-MONOMER.
    ECOL316407:JW0228-MONOMER.
    MetaCyc:GPT-MONOMER.
    BRENDAi2.4.2.22. 2026.
    UniPathwayiUPA00602; UER00658.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xanthine phosphoribosyltransferase (EC:2.4.2.22)
    Alternative name(s):
    Xanthine-guanine phosphoribosyltransferase
    Short name:
    XGPRT
    Gene namesi
    Name:gpt
    Synonyms:gpp, gxu
    Ordered Locus Names:b0238, JW0228
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10414. gpt.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • plasma membrane Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591C → A: No effect on catalytic activity; increased stability. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 152152Xanthine phosphoribosyltransferasePRO_0000139666Add
    BLAST

    Proteomic databases

    PaxDbiP0A9M5.
    PRIDEiP0A9M5.

    2D gel databases

    SWISS-2DPAGEP0A9M5.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    blcP0A9011EBI-909091,EBI-1114945

    Protein-protein interaction databases

    IntActiP0A9M5. 1 interaction.
    STRINGi511145.b0238.

    Structurei

    Secondary structure

    1
    152
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63Combined sources
    Helixi9 – 2315Combined sources
    Helixi26 – 283Combined sources
    Beta strandi30 – 367Combined sources
    Turni37 – 393Combined sources
    Helixi40 – 5011Combined sources
    Beta strandi55 – 617Combined sources
    Beta strandi72 – 754Combined sources
    Beta strandi78 – 803Combined sources
    Beta strandi84 – 918Combined sources
    Helixi97 – 1037Combined sources
    Beta strandi107 – 1148Combined sources
    Helixi116 – 1216Combined sources
    Beta strandi123 – 1286Combined sources
    Beta strandi134 – 1363Combined sources
    Helixi138 – 1403Combined sources
    Beta strandi141 – 1455Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A95X-ray2.00A/B/C/D1-152[»]
    1A96X-ray2.00A/B/C/D1-152[»]
    1A97X-ray2.60A/B/C/D3-150[»]
    1A98X-ray2.25A/B1-152[»]
    1NULX-ray1.80A/B1-152[»]
    ProteinModelPortaliP0A9M5.
    SMRiP0A9M5. Positions 3-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9M5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 3825-phosphoribose 1-diphosphate binding
    Regioni92 – 9655-phosphoribose 1-diphosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0503.
    HOGENOMiHOG000226805.
    InParanoidiP0A9M5.
    KOiK00769.
    OMAiKAHFATV.
    OrthoDBiEOG6H1Q23.
    PhylomeDBiP0A9M5.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    HAMAPiMF_01903. XGPRT.
    InterProiIPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR023747. Xanthine_Guanine_PRibTrfase.
    [Graphical view]
    PfamiPF00156. Pribosyltran. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A9M5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSEKYIVTWD MLQIHARKLA SRLMPSEQWK GIIAVSRGGL VPGALLAREL
    60 70 80 90 100
    GIRHVDTVCI SSYDHDNQRE LKVLKRAEGD GEGFIVIDDL VDTGGTAVAI
    110 120 130 140 150
    REMYPKAHFV TIFAKPAGRP LVDDYVVDIP QDTWIEQPWD MGVVFVPPIS

    GR
    Length:152
    Mass (Da):16,971
    Last modified:July 21, 1986 - v1
    Checksum:iF0AD813127E7200D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti122 – 1221V → G in AAA23933 (PubMed:3540961).Curated

    Mass spectrometryi

    Molecular mass is 16805 Da from positions 1 - 152. Determined by API. The measured mass is that of mutant Ala-59.1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X00221 Genomic DNA. Translation: CAA25040.1.
    X00222 Genomic DNA. Translation: CAA25041.1.
    M13422 Genomic DNA. Translation: AAA23928.1.
    M12907 Genomic DNA. Translation: AAA23932.1.
    M15035 Genomic DNA. Translation: AAA23933.1.
    U70214 Genomic DNA. Translation: AAB08658.1.
    U00096 Genomic DNA. Translation: AAC73342.1.
    AP009048 Genomic DNA. Translation: BAA77907.1.
    M10382 Genomic DNA. Translation: AAA23931.1.
    PIRiA00587. RTECGX.
    RefSeqiNP_414773.1. NC_000913.3.
    WP_001291990.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73342; AAC73342; b0238.
    BAA77907; BAA77907; BAA77907.
    GeneIDi944817.
    KEGGieco:b0238.
    PATRICi32115591. VBIEscCol129921_0240.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X00221 Genomic DNA. Translation: CAA25040.1.
    X00222 Genomic DNA. Translation: CAA25041.1.
    M13422 Genomic DNA. Translation: AAA23928.1.
    M12907 Genomic DNA. Translation: AAA23932.1.
    M15035 Genomic DNA. Translation: AAA23933.1.
    U70214 Genomic DNA. Translation: AAB08658.1.
    U00096 Genomic DNA. Translation: AAC73342.1.
    AP009048 Genomic DNA. Translation: BAA77907.1.
    M10382 Genomic DNA. Translation: AAA23931.1.
    PIRiA00587. RTECGX.
    RefSeqiNP_414773.1. NC_000913.3.
    WP_001291990.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A95X-ray2.00A/B/C/D1-152[»]
    1A96X-ray2.00A/B/C/D1-152[»]
    1A97X-ray2.60A/B/C/D3-150[»]
    1A98X-ray2.25A/B1-152[»]
    1NULX-ray1.80A/B1-152[»]
    ProteinModelPortaliP0A9M5.
    SMRiP0A9M5. Positions 3-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP0A9M5. 1 interaction.
    STRINGi511145.b0238.

    2D gel databases

    SWISS-2DPAGEP0A9M5.

    Proteomic databases

    PaxDbiP0A9M5.
    PRIDEiP0A9M5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73342; AAC73342; b0238.
    BAA77907; BAA77907; BAA77907.
    GeneIDi944817.
    KEGGieco:b0238.
    PATRICi32115591. VBIEscCol129921_0240.

    Organism-specific databases

    EchoBASEiEB0409.
    EcoGeneiEG10414. gpt.

    Phylogenomic databases

    eggNOGiCOG0503.
    HOGENOMiHOG000226805.
    InParanoidiP0A9M5.
    KOiK00769.
    OMAiKAHFATV.
    OrthoDBiEOG6H1Q23.
    PhylomeDBiP0A9M5.

    Enzyme and pathway databases

    UniPathwayiUPA00602; UER00658.
    BioCyciEcoCyc:GPT-MONOMER.
    ECOL316407:JW0228-MONOMER.
    MetaCyc:GPT-MONOMER.
    BRENDAi2.4.2.22. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A9M5.
    PROiP0A9M5.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    HAMAPiMF_01903. XGPRT.
    InterProiIPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR023747. Xanthine_Guanine_PRibTrfase.
    [Graphical view]
    PfamiPF00156. Pribosyltran. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequence of the Escherichia coli xanthine-guanine phosphoribosyl transferase gene."
      Pratt D., Subramani S.
      Nucleic Acids Res. 11:8817-8823(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence of the xanthine guanine phosphoribosyl transferase gene of E. coli."
      Richardson K.K., Fostel J., Skopek T.R.
      Nucleic Acids Res. 11:8809-8816(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Structural and functional organization of the gpt gene region of Escherichia coli."
      Nueesch J., Schuemperli D.
      Gene 32:243-249(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Nucleotide sequence and analysis of deletion mutants of the Escherichia coli gpt gene in plasmid pSV2 gpt."
      Jagadeeswaran P., Ashman C.R., Roberts S., Langenberg J.
      Gene 31:309-313(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "DNA base changes and alkylation following in vivo exposure of Escherichia coli to N-methyl-N-nitrosourea or N-ethyl-N-nitrosourea."
      Richardson K.K., Richardson F.C., Crosby R.M., Swenberg J.A., Skopek T.R.
      Proc. Natl. Acad. Sci. U.S.A. 84:344-348(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
      Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    9. "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.
    10. "Factors governing the expression of a bacterial gene in mammalian cells."
      Mulligan R.C., Berg P.
      Mol. Cell. Biol. 1:449-459(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
    11. "Crystal structure of Escherichia coli xanthine phosphoribosyltransferase."
      Vos S., de Jersey J., Martin J.L.
      Biochemistry 36:4125-4134(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 66-76, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-59 IN COMPLEX WITH MAGNESIUM, MASS SPECTROMETRY, COFACTOR, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    12. "Purification and characterization of Escherichia coli xanthine-guanine phosphoribosyltransferase produced by plasmid pSV2gpt."
      Deo S.S., Tseng W.C., Saini R., Coles R.S., Athwal R.S.
      Biochim. Biophys. Acta 839:233-239(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    13. "Crystallization and preliminary X-ray crystallographic studies of Escherichia coli xanthine phosphoribosyltransferase."
      Vos S., de Jersey J., Martin J.L.
      J. Struct. Biol. 116:330-334(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-59, CRYSTALLIZATION OF WILD-TYPE AND OF MUTANT ALA-59.
    14. "Structures of free and complexed forms of Escherichia coli xanthine-guanine phosphoribosyltransferase."
      Vos S., Parry R.J., Burns M.R., de Jersey J., Martin J.L.
      J. Mol. Biol. 282:875-889(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT ALA-59 IN COMPLEXES WITH GUANINE; XANTHINE; 5-PHOSPHO-ALPHA-D-RIBOSE-1-DIPHOSPHATE AND MAGNESIUM, SUBUNIT.

    Entry informationi

    Entry nameiXGPT_ECOLI
    AccessioniPrimary (citable) accession number: P0A9M5
    Secondary accession number(s): P00501
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: July 22, 2015
    This is version 92 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

    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

    External Data

    Dasty 3

    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 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.