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Q9RN37 (USHA_SALPU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein UshA

Including the following 2 domains:

  1. UDP-sugar hydrolase
    EC=3.6.1.45
    Alternative name(s):
    UDP-sugar diphosphatase
    UDP-sugar pyrophosphatase
  2. 5'-nucleotidase
    Short name=5'-NT
    EC=3.1.3.5
Gene names
Name:ushA
OrganismSalmonella pullorum
Taxonomic identifier605 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Periplasm By similarity.

Sequence similarities

Belongs to the 5'-nucleotidase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMetal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processnucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function5'-nucleotidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

UDP-sugar diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 By similarity
Chain26 – 550525Protein UshA
PRO_0000000032

Regions

Region498 – 5047Substrate binding By similarity

Sites

Metal binding411Zinc 1 By similarity
Metal binding431Zinc 1 By similarity
Metal binding841Zinc 1 By similarity
Metal binding841Zinc 2 By similarity
Metal binding1161Zinc 2 By similarity
Metal binding2171Zinc 2 By similarity
Metal binding2521Zinc 2 By similarity
Metal binding2541Zinc 1 By similarity
Binding site4291Substrate By similarity
Site1171Transition state stabilizer By similarity
Site1201Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond258 ↔ 275 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RN37 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 655BC7E8F0D4F62F

FASTA55060,604
        10         20         30         40         50         60 
MKFLKRGVAL ALLAAFALTT QPAQAYEKDK TYKITILHTN DHHGHFWRSE YGEYGLAAQK 

        70         80         90        100        110        120 
TLVDSIRKEV AQEGGGVLLL SGGDINTGVP ESDLQDAEPD FRGMNLIGYD AMAVGNHEFD 

       130        140        150        160        170        180 
NPLTVLRQQE KWAKFPFLSA NIYQKSTGER LFKPWAIFTR QDIKIAVIGL TTDDTAKIGN 

       190        200        210        220        230        240 
PEYFTDIEFR KPAEEAKVVI QELNMNEKPD VIIATTHMGH YDNGDHGSNA PGDVEMARSL 

       250        260        270        280        290        300 
PAGSLAMIVG GHSQDPVCMA SENKKQVNYV PGTPCAPDKQ NGIWIVQAHE WGKYVGRADF 

       310        320        330        340        350        360 
EFRNGEMKMV NYQLIPVNLK KKVTWDNGKS ERVLYTPEIA ENPQMLLLLT PFQNKGKVQL 

       370        380        390        400        410        420 
EVKIGSVNGL LEGDRSKVRF VQTNMGRVIL AAQIARTGAD FGVMSGGGIR DSIEAGDITY 

       430        440        450        460        470        480 
KSVLKVQPFG NIVVYADMSG KEVVDYLTRV AQMKPDSGAY PQLANVSFVA KEGKLTDLKI 

       490        500        510        520        530        540 
KGEPVDPAKT YRMATLSFNA TGGDGYPRID NKPGYVNTGF IDAEVLKEFI QQNSPLDAAA 

       550 
FTPKGEVSWL 

« Hide

References

[1]"The cryptic ushA gene (ushA(c)) in natural isolates of Salmonella enterica (serotype Typhimurium) has been inactivated by a single missense mutation."
Innes D., Beacham I.R., Beven C.-A., Douglas M., Laird M.W., Joly J.C., Burns D.M.
Microbiology 147:1887-1896(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF188727 Genomic DNA. Translation: AAF05581.1.

3D structure databases

ProteinModelPortalQ9RN37.
SMRQ9RN37. Positions 26-549.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9RN37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.780.10. 1 hit.
InterProIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
[Graphical view]
PANTHERPTHR11575. PTHR11575. 1 hit.
PfamPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR01607. APYRASEFAMLY.
SUPFAMSSF55816. SSF55816. 1 hit.
PROSITEPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUSHA_SALPU
AccessionPrimary (citable) accession number: Q9RN37
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families