Q9R5V5 (NTD_LACLE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 51.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nucleoside deoxyribosyltransferase Short name=N-deoxyribosyltransferase EC=2.4.2.6 | ||
| Gene names |
| ||
| Organism | Lactobacillus leichmannii | ||
| Taxonomic identifier | 28039 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus![]() |
Protein attributes
| Sequence length | 157 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the cleavage of the glycosidic bond of 2'-deoxyribonucleosides and the transfer of the deoxyribosyl moiety to an acceptor purine or pyrimidine base. Ref.1 Ref.2 |
| Catalytic activity | 2-deoxy-D-ribosyl-base1 + base2 = 2-deoxy-D-ribosyl-base2 + base1. Ref.1 |
| Pathway | Nucleotide metabolism; nucleotide salvage pathway. Ref.1 Ref.2 |
| Subunit structure | Homohexamer. Ref.2 |
| Sequence similarities | Belongs to the nucleoside deoxyribosyltransferase family. |
| Caution | Was originally (Ref.1) thought to originate from E.coli. |
| Biophysicochemical properties | pH dependence: Optimum pH is 6.0. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Molecular function | Transferase |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | deoxyribonucleoside monophosphate catabolic process Inferred from electronic annotation. Source: InterPro nucleotide salvageInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | deoxyribonucleoside 5'-monophosphate N-glycosidase activity Inferred from electronic annotation. Source: InterPro nucleoside deoxyribosyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.1 | ||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 157 | 156 | Nucleoside deoxyribosyltransferase | PRO_0000220067 | |||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||
| Active site | 98 | 1 | Nucleophile Ref.1 | ||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 98 | 1 | E → A: Loss of transferase activity. Ref.1 | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 6 – 9 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 15 – 30 | 16 | |||||||||||||||||||||||||||||||||||||||
| Helix | 36 – 38 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 42 – 44 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 47 – 49 | 3 | |||||||||||||||||||||||||||||||||||||||
| Turn | 52 – 54 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 56 – 60 | 5 | |||||||||||||||||||||||||||||||||||||||
| Helix | 62 – 77 | 16 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 79 – 85 | 7 | |||||||||||||||||||||||||||||||||||||||
| Helix | 88 – 90 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 104 | 12 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 108 – 113 | 6 | |||||||||||||||||||||||||||||||||||||||
| Helix | 115 – 117 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 124 – 129 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 131 – 135 | 5 | |||||||||||||||||||||||||||||||||||||||
| Helix | 136 – 138 | 3 | |||||||||||||||||||||||||||||||||||||||
| Turn | 139 – 141 | 3 | |||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Identification of the active site nucleophile in nucleoside 2-deoxyribosyltransferase as glutamic acid 98." Porter D.J.T., Merrill B.M., Short S.A. J. Biol. Chem. 270:15551-15556(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, FUNCTION, ACTIVE SITE, MUTAGENESIS OF GLU-98. |
| [2] | "Crystal structures of nucleoside 2-deoxyribosyltransferase in native and ligand-bound forms reveal architecture of the active site." Armstrong S.R., Cook W.J., Short S.A., Ealick S.E. Structure 4:97-107(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). |
Cross-references
3D structure databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q9R5V5. | ||||||||||||||||||||||||
| SMR | Q9R5V5. Positions 2-157. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| UniPathway | UPA00312. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR007710. Nucleoside_deoxyribTrfase. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF05014. Nuc_deoxyrib_tr. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| EvolutionaryTrace | Q9R5V5. | ||||||||||||||||||||||||
Entry information
| Entry name | NTD_LACLE | ||||||||
| Accession | Primary (citable) accession number: Q9R5V5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
