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P0A9M5 (XGPT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xanthine phosphoribosyltransferase

EC=2.4.2.22
Alternative name(s):
Xanthine-guanine phosphoribosyltransferase
Short name=XGPRT
Gene names
Name:gpt
Synonyms:gpp, gxu
Ordered Locus Names:b0238, JW0228
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts on guanine, xanthine and to a lesser extent hypoxanthine. Ref.11

Catalytic activity

XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine. HAMAP-Rule MF_01903

Cofactor

Binds 1 magnesium ion per subunit. Ref.11

Enzyme regulation

Inhibited by thioguanine, GMP and, to a lesser extent, by thioxanthine, azaxanthine and azaguanine. Ref.12

Pathway

Purine metabolism; XMP biosynthesis via salvage pathway; XMP from xanthine: step 1/1. HAMAP-Rule MF_01903

Subunit structure

Homotetramer. Ref.11 Ref.14

Subcellular location

Cell inner membrane; Peripheral membrane protein Probable HAMAP-Rule MF_01903.

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=4.3 µM for guanine Ref.11 Ref.12

KM=30.5 µM for xanthine

KM=90.8 µM for hypoxanthine

Mass spectrometry

Molecular mass is 16805 Da from positions 1 - 152. Determined by API. The measured mass is that of mutant Ala-59. Ref.11

Binary interactions

With

Entry

#Exp.

IntAct

Notes

blcP0A9011EBI-909091,EBI-1114945

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Xanthine phosphoribosyltransferase HAMAP-Rule MF_01903
PRO_0000139666

Regions

Region37 – 3825-phosphoribose 1-diphosphate binding HAMAP-Rule MF_01903
Region92 – 9655-phosphoribose 1-diphosphate binding HAMAP-Rule MF_01903

Sites

Metal binding891Magnesium
Binding site6915-phosphoribose 1-diphosphate
Binding site921Xanthine
Binding site1351Xanthine; via amide nitrogen and carbonyl oxygen

Experimental info

Mutagenesis591C → A: No effect on catalytic activity; increased stability. Ref.13
Sequence conflict1221V → G in AAA23933. Ref.5

Secondary structure

................................ 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9M5 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F0AD813127E7200D

FASTA15216,971
        10         20         30         40         50         60 
MSEKYIVTWD MLQIHARKLA SRLMPSEQWK GIIAVSRGGL VPGALLAREL GIRHVDTVCI 

        70         80         90        100        110        120 
SSYDHDNQRE LKVLKRAEGD GEGFIVIDDL VDTGGTAVAI REMYPKAHFV TIFAKPAGRP 

       130        140        150 
LVDDYVVDIP QDTWIEQPWD MGVVFVPPIS GR 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRRTECGX. A00587.
RefSeqNP_414773.1. NC_000913.3.
YP_488533.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0A9M5.
SMRP0A9M5. Positions 3-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A9M5. 1 interaction.
STRING511145.b0238.

2D gel databases

SWISS-2DPAGEP0A9M5.

Proteomic databases

PaxDbP0A9M5.
PRIDEP0A9M5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73342; AAC73342; b0238.
BAA77907; BAA77907; BAA77907.
GeneID12931995.
944817.
KEGGecj:Y75_p0229.
eco:b0238.
PATRIC32115591. VBIEscCol129921_0240.

Organism-specific databases

EchoBASEEB0409.
EcoGeneEG10414. gpt.

Phylogenomic databases

eggNOGCOG0503.
HOGENOMHOG000226805.
KOK00769.
OMAKAHFATV.
OrthoDBEOG6H1Q23.
PhylomeDBP0A9M5.
ProtClustDBPRK09177.

Enzyme and pathway databases

BioCycEcoCyc:GPT-MONOMER.
ECOL316407:JW0228-MONOMER.
MetaCyc:GPT-MONOMER.
UniPathwayUPA00602; UER00658.

Gene expression databases

GenevestigatorP0A9M5.

Family and domain databases

HAMAPMF_01903. XGPRT.
InterProIPR000836. PRibTrfase_dom.
IPR023747. Xanthine_Guanine_PRibTrfase.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A9M5.
PROP0A9M5.

Entry information

Entry nameXGPT_ECOLI
AccessionPrimary (citable) accession number: P0A9M5
Secondary accession number(s): P00501
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene