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P0A9M5

- XGPT_ECOLI

UniProt

P0A9M5 - XGPT_ECOLI

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Protein

Xanthine phosphoribosyltransferase

Gene

gpt

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Binds 1 magnesium 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

Pathwayi

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

  1. hypoxanthine phosphoribosyltransferase activity Source: EcoCyc
  2. magnesium ion binding Source: UniProtKB-HAMAP
  3. xanthine phosphoribosyltransferase activity Source: EcoCyc

GO - Biological processi

  1. GMP salvage Source: EcoCyc
  2. IMP salvage Source: EcoCyc
  3. 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.
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10414. gpt.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. plasma membrane Source: UniProtKB-HAMAP
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.

Expressioni

Gene expression databases

GenevestigatoriP0A9M5.

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 – 63
Helixi9 – 2315
Helixi26 – 283
Beta strandi30 – 367
Turni37 – 393
Helixi40 – 5011
Beta strandi55 – 617
Beta strandi72 – 754
Beta strandi78 – 803
Beta strandi84 – 918
Helixi97 – 1037
Beta strandi107 – 1148
Helixi116 – 1216
Beta strandi123 – 1286
Beta strandi134 – 1363
Helixi138 – 1403
Beta strandi141 – 1455

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiMYTRQLA.
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:
EMBL
GenBank
DDBJ
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.
YP_488533.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73342; AAC73342; b0238.
BAA77907; BAA77907; BAA77907.
GeneIDi12931995.
944817.
KEGGiecj:Y75_p0229.
eco:b0238.
PATRICi32115591. VBIEscCol129921_0240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A00587. RTECGX.
RefSeqi NP_414773.1. NC_000913.3.
YP_488533.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A95 X-ray 2.00 A/B/C/D 1-152 [» ]
1A96 X-ray 2.00 A/B/C/D 1-152 [» ]
1A97 X-ray 2.60 A/B/C/D 3-150 [» ]
1A98 X-ray 2.25 A/B 1-152 [» ]
1NUL X-ray 1.80 A/B 1-152 [» ]
ProteinModelPortali P0A9M5.
SMRi P0A9M5. Positions 3-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A9M5. 1 interaction.
STRINGi 511145.b0238.

2D gel databases

SWISS-2DPAGE P0A9M5.

Proteomic databases

PaxDbi P0A9M5.
PRIDEi P0A9M5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73342 ; AAC73342 ; b0238 .
BAA77907 ; BAA77907 ; BAA77907 .
GeneIDi 12931995.
944817.
KEGGi ecj:Y75_p0229.
eco:b0238.
PATRICi 32115591. VBIEscCol129921_0240.

Organism-specific databases

EchoBASEi EB0409.
EcoGenei EG10414. gpt.

Phylogenomic databases

eggNOGi COG0503.
HOGENOMi HOG000226805.
InParanoidi P0A9M5.
KOi K00769.
OMAi MYTRQLA.
OrthoDBi EOG6H1Q23.
PhylomeDBi P0A9M5.

Enzyme and pathway databases

UniPathwayi UPA00602 ; UER00658 .
BioCyci EcoCyc:GPT-MONOMER.
ECOL316407:JW0228-MONOMER.
MetaCyc:GPT-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A9M5.
PROi P0A9M5.

Gene expression databases

Genevestigatori P0A9M5.

Family and domain databases

Gene3Di 3.40.50.2020. 1 hit.
HAMAPi MF_01903. XGPRT.
InterProi IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR023747. Xanthine_Guanine_PRibTrfase.
[Graphical view ]
Pfami PF00156. Pribosyltran. 1 hit.
[Graphical view ]
SUPFAMi SSF53271. SSF53271. 1 hit.
PROSITEi PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 86 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