Reviewed,
UniProtKB/Swiss-Prot Q56878 (USHA_YERE8)
Last modified
November 3, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein ushA Including the following 2 domains: 1- Recommended name: UDP-sugar hydrolase EC=3.6.1.45 Alternative name(s): UDP-sugar pyrophosphatase UDP-sugar diphosphatase 2- Recommended name: 5'-nucleotidase Short name=5'-NT EC=3.1.3.5 | ||||
| Gene names |
| ||||
| Organism | Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 393305 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia |
Protein attributes
| Sequence length | 550 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 external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell By similarity. |
| Catalytic activity | UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate. A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. |
| Cofactor | Divalent cations. Most likely cobalt By similarity. |
| Subcellular location | Periplasm Potential. |
| Sequence similarities | Belongs to the 5'-nucleotidase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Cobalt Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | nucleotide catabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 5'-nucleotidase activity Inferred from electronic annotation. Source: EC UDP-sugar diphosphatase activityInferred from electronic annotation. Source: EC cobalt 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 – 25 | 25 | Potential | ||||||||
| Chain | 26 – 550 | 525 | Protein ushA | PRO_0000000034 | |||||||
Regions | |||||||||||
| Region | 375 – 379 | 5 | Substrate binding By similarity | ||||||||
| Region | 498 – 504 | 7 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Metal binding | 41 | 1 | Divalent metal cation 1 By similarity | ||||||||
| Metal binding | 43 | 1 | Divalent metal cation 1 By similarity | ||||||||
| Metal binding | 84 | 1 | Divalent metal cation 1 By similarity | ||||||||
| Metal binding | 84 | 1 | Divalent metal cation 2 By similarity | ||||||||
| Metal binding | 116 | 1 | Divalent metal cation 2 By similarity | ||||||||
| Metal binding | 217 | 1 | Divalent metal cation 2 By similarity | ||||||||
| Metal binding | 252 | 1 | Divalent metal cation 2 By similarity | ||||||||
| Metal binding | 254 | 1 | Divalent metal cation 1 By similarity | ||||||||
| Site | 117 | 1 | Transition state stabilizer By similarity | ||||||||
| Site | 120 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 258 ↔ 275 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 24 | 1 | V → A in AAC60782. Ref.2 | ||||||||
| Sequence conflict | 47 | 1 | W → C in AAC60782. Ref.2 | ||||||||
| Sequence conflict | 72 – 83 | 12 | AAGGS…LLSGG → RSRGKLVVALRW in AAC60782. Ref.2 | ||||||||
| Sequence conflict | 126 | 1 | Missing in AAC60782. Ref.2 | ||||||||
| Sequence conflict | 129 – 130 | 2 | QE → HQ in AAC60782. Ref.2 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081." Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. Prentice M.B.PLoS Genet. 2:2039-2051(2006) [PubMed: 17173484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | Zhang L., Toivanen P., Skurnik M. Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-374. |
Cross-references
Sequence databases | |
|---|---|
| AM286415 Genomic DNA. Translation: CAL13101.1. U46859 Genomic DNA. Translation: AAC60782.1. Different initiation. | |
| RefSeq | YP_001007248.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2USH based on UniProtKB P07024. |
| SMR | Q56878. Positions 26-550. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q56878. |
Genome annotation databases | |
| GeneID | 4714553. |
| GenomeReviews | Gene locus YE3066 in contig AM286415_GR. |
| KEGG | yen:YE3066. |
| NMPDR | fig|630.2.peg.2998. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | QADYVPG. |
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. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | USHA_YERE8 | ||||||||
| Accession | Primary (citable) accession number: Q56878 Secondary accession number(s): A1JN00 | ||||||||
| 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


