Pyrimidine-nucleoside phosphorylase

Details

Name
Pyrimidine-nucleoside phosphorylase
Synonyms
  • 2.4.2.2
  • pyn
  • PYNP
Gene Name
pdp
Organism
Geobacillus stearothermophilus
Amino acid sequence
>lcl|BSEQ0012152|Pyrimidine-nucleoside phosphorylase
MRMVDLIEKKRDGHALTKEEIQFIIEGYTKGDIPDYQMSALAMAIFFRGMNEEETAELTM
AMVHSGDTIDLSRIEGIKVDKHSTGGVGDTTTLVLGPLVASVGVPVAKMSGRGLGHTGGT
IDKLESVPGFHVEITNDEFIDLVNKNKIAVVGQSGNLTPADKKLYALRDVTATVNSIPLI
ASSIMSKKIAAGADAIVLDVKTGVGAFMKDLNDAKALAKAMVDIGNRVGRKTMAIISDMS
QPLGYAIGNALEVKEAIDTLKGEGPEDFQELCLVLGSHMVYLAEKASSLEEARHMLEKAM
KDGSALQTFKTFLAAQGGDASVVDDPSKLPQAKYIIELEAKEDGYVSEIVADAVGTAAMW
LGAGRATKESTIDLAVGLVLRKKVGDAVKKGESLVTIYSNREQVDDVKQKLYENIRISAT
PVQAPTLIYDKIS
Number of residues
433
Molecular Weight
46331.92
Theoretical pI
5.04
GO Classification
Functions
metal ion binding / phosphorylase activity / pyrimidine-nucleoside phosphorylase activity
Processes
pyrimidine nucleobase metabolic process / pyrimidine nucleoside metabolic process
General Function
Pyrimidine-nucleoside phosphorylase activity
Specific Function
Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0006016|1302 bp
ATGAGAATGGTCGATTTAATTGAGAAAAAACGTGATGGTCATGCGTTAACGAAAGAAGAA
ATTCAGTTTATTATTGAAGGTTACACAAAAGGCGATATTCCTGATTATCAAATGAGCGCA
TTAGCGATGGCGATTTTTTTCCGCGGCATGAATGAAGAAGAGACAGCGGAATTGACGATG
GCGATGGTGCATTCAGGCGATACGATCGACCTTTCGCGAATTGAAGGAATTAAAGTAGAC
AAACATTCAACGGGCGGAGTGGGCGATACAACAACGTTAGTGCTTGGCCCTCTTGTCGCC
TCCGTCGGTGTTCCGGTTGCGAAAATGTCTGGGCGCGGCCTTGGACATACGGGTGGAACG
ATCGACAAACTAGAATCGGTGCCAGGTTTTCACGTTGAAATTACGAACGATGAATTTATC
GATCTTGTCAATAAAAATAAAATTGCCGTTGTCGGTCAGTCTGGTAATTTGACGCCAGCG
GACAAAAAGTTGTATGCGCTTCGTGATGTGACGGCAACGGTCAATAGCATTCCGTTAATT
GCCTCATCGATTATGAGCAAAAAAATTGCCGCAGGGGCAGATGCGATCGTACTTGACGTA
AAAACAGGTGTGGGCGCGTTTATGAAAGATTTAAACGATGCAAAAGCATTAGCGAAAGCG
ATGGTCGATATCGGAAATCGGGTTGGGCGTAAAACGATGGCAATTATTTCTGATATGAGC
CAGCCGCTTGGTTATGCCATTGGAAATGCGCTTGAAGTGAAAGAAGCGATTGATACGTTA
AAAGGAGAAGGTCCAGAAGATTTCCAAGAGCTGTGCTTAGTGCTTGGTAGCCACATGGTA
TATTTAGCGGAAAAAGCATCTTCGCTTGAAGAAGCTCGTCATATGTTAGAAAAAGCGATG
AAAGACGGTTCAGCCCTTCAAACATTTAAAACGTTCTTAGCTGCGCAAGGTGGCGATGCA
TCTGTTGTCGATGACCCAAGCAAATTGCCGCAAGCAAAATATATTATTGAACTAGAAGCG
AAAGAAGATGGATACGTATCCGAAATTGTCGCGGATGCGGTCGGAACGGCGGCGATGTGG
CTTGGTGCAGGGCGAGCGACGAAAGAATCAACGATCGATTTAGCTGTCGGTCTCGTGCTT
CGCAAAAAAGTCGGCGATGCGGTGAAAAAAGGTGAATCGCTCGTTACAATTTACAGCAAC
CGTGAACAAGTGGATGATGTAAAACAAAAACTATATGAAAACATTCGTATTTCAGCAACA
CCTGTTCAAGCTCCAACATTAATTTACGATAAAATTTCGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP77836
UniProtKB Entry NamePDP_GEOSE
GenBank Gene IDD87961
General References
  1. Okuyama K, Hamamoto T, Noguchi T, Midorikawa Y: Molecular cloning and expression of the pyrimidine nucleoside phosphorylase gene from Bacillus stearothermophilus TH 6-2. Biosci Biotechnol Biochem. 1996 Oct;60(10):1655-9. [Article]
  2. Hamamoto T, Noguchi T, Midorikawa Y: Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2. Biosci Biotechnol Biochem. 1996 Jul;60(7):1179-80. [Article]
  3. Pugmire MJ, Ealick SE: The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation. Structure. 1998 Nov 15;6(11):1467-79. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03419Uracilexperimental, investigationalunknownDetails