Nucleoside 2-deoxyribosyltransferase
Details
- Name
- Nucleoside 2-deoxyribosyltransferase
- Synonyms
- ndtA
- Nucleoside deoxyribosyltransferase-I
- Purine trans deoxyribosylase
- Gene Name
- ptd
- Organism
- Lactobacillus helveticus
- Amino acid sequence
>lcl|BSEQ0011910|Nucleoside 2-deoxyribosyltransferase MKAVVPTGKIYLGSPFYSDAQRERAAKAKELLAKNPSIAHVFFPFDDGFTDPDEKNPEIG GIRSMVWRDATYQNDLTGISNATCGVFLYDMDQLDDGSAFEIGFMRAMHKPVILVPFTEH PEKEKKMNLMIAQGVTTIIDGNTEFEKLADYNFNECPSNPVRGYGIY
- Number of residues
- 167
- Molecular Weight
- 18713.08
- Theoretical pI
- 4.7
- GO Classification
- Functionsdeoxyribonucleoside 5'-monophosphate N-glycosidase activity / nucleoside deoxyribosyltransferase activityProcessesdeoxyribonucleoside monophosphate catabolic process
- General Function
- Nucleoside deoxyribosyltransferase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Nuc_deoxyrib_tr (PF05014)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0005306|504 bp ATGAAAGCAGTAGTTCCAACAGGAAAAATTTATTTAGGCTCACCATTTTACAGCGATGCT CAAAGAGAAAGAGCAGCTAAGGCAAAAGAGTTGTTAGCAAAAAATCCAAGCATCGCGCAC GTCTTCTTCCCCTTTGATGATGGTTTCACCGATCCTGATGAAAAGAATCCTGAAATTGGC GGCATCAGAAGCATGGTTTGGCGGGATGCAACTTACCAAAATGATTTAACTGGTATTTCG AATGCCACTTGTGGCGTCTTCTTATATGATATGGATCAATTAGATGACGGCTCTGCCTTT GAAATTGGCTTCATGCGTGCGATGCATAAGCCGGTGATCTTGGTGCCATTCACTGAGCAT CCCGAAAAAGAAAAGAAAATGAACCTGATGATCGCACAAGGCGTAACCACCATCATTGAT GGCAATACTGAATTTGAAAAACTAGCTGATTATAACTTCAACGAATGTCCTTCTAATCCA GTTCGCGGTTACGGTATCTATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q8RLY5 UniProtKB Entry Name Q8RLY5_LACHE GenBank Gene ID AY064166 - General References
- Kaminski PA: Functional cloning, heterologous expression, and purification of two different N-deoxyribosyltransferases from Lactobacillus helveticus. J Biol Chem. 2002 Apr 26;277(17):14400-7. Epub 2002 Feb 8. [Article]
- Anand R, Kaminski PA, Ealick SE: Structures of purine 2'-deoxyribosyltransferase, substrate complexes, and the ribosylated enzyme intermediate at 2.0 A resolution. Biochemistry. 2004 Mar 9;43(9):2384-93. [Article]