Reviewed,
UniProtKB/Swiss-Prot Q8DFG4 (5NTD_VIBVU)
Last modified
October 13, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 5'-nucleotidase EC=3.1.3.5 | ||||
| Gene names |
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| Organism | Vibrio vulnificus [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 672 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
Protein attributes
| Sequence length | 553 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Degradation of extracellular 5'-nucleotides for nutritional needs By similarity. |
| Catalytic activity | A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. |
| Cofactor | Chloride By similarity. Magnesium By similarity. |
| Subcellular location | Cell outer membrane; Lipid-anchor Probable. |
| Sequence similarities | Belongs to the 5'-nucleotidase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Cell outer membrane Membrane |
| Domain | Signal |
| Ligand | Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Lipoprotein Palmitate |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | nucleotide catabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell outer membraneInferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 5'-nucleotidase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleotide bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Potential | ||||||
| Chain | 22 – 553 | 532 | 5'-nucleotidase | PRO_0000000030 | |||||
Regions | |||||||||
| Region | 501 – 507 | 7 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 45 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 47 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 88 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 88 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 120 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 221 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 256 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 258 | 1 | Divalent metal cation 1 By similarity | ||||||
| Binding site | 432 | 1 | Substrate By similarity | ||||||
| Site | 121 | 1 | Transition state stabilizer By similarity | ||||||
| Site | 124 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Lipidation | 22 | 1 | N-palmitoyl cysteine Probable | ||||||
| Lipidation | 22 | 1 | S-diacylglycerol cysteine Probable | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| AE016795 Genomic DNA. Translation: AAO08784.1. Different initiation. | |
| RefSeq | NP_759257.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2USH based on UniProtKB P07024. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1177201. |
| GenomeReviews | Gene locus VV1_0248 in contig AE016795_GR. |
| KEGG | vvu:VV1_0248. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8DFG4. |
Enzyme and pathway databases | |
| BioCyc | VVUL216895:VV1_0248-MON. |
| BRENDA | 3.1.3.5. 277169. |
Family and domain databases | |
| InterPro | IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR004843. M-pesterase. [Graphical view] |
| Gene3D | G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit. |
| PANTHER | PTHR11575. 5_nucleotidase. 1 hit. |
| Pfam | PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view] |
| PRINTS | PR01607. APYRASEFAMLY. |
| PROSITE | PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. PS51257. PROKAR_LIPOPROTEIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | 5NTD_VIBVU | ||||||||
| Accession | Primary (citable) accession number: Q8DFG4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


