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Q56878 (USHA_YERE8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. 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
Ordered Locus Names:YE3066
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

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

Divalent cations. Most likely cobalt By similarity.

Subcellular location

Periplasm Potential.

Sequence similarities

Belongs to the 5'-nucleotidase family.

Sequence caution

The sequence AAC60782.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandCobalt
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termComplete proteome
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 Potential
Chain26 – 550525Protein UshA
PRO_0000000034

Regions

Region375 – 3795Substrate binding By similarity
Region498 – 5047Substrate binding By similarity

Sites

Metal binding411Divalent metal cation 1 By similarity
Metal binding431Divalent metal cation 1 By similarity
Metal binding841Divalent metal cation 1 By similarity
Metal binding841Divalent metal cation 2 By similarity
Metal binding1161Divalent metal cation 2 By similarity
Metal binding2171Divalent metal cation 2 By similarity
Metal binding2521Divalent metal cation 2 By similarity
Metal binding2541Divalent metal cation 1 By similarity
Site1171Transition state stabilizer By similarity
Site1201Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond258 ↔ 275 By similarity

Experimental info

Sequence conflict241V → A in AAC60782. Ref.2
Sequence conflict471W → C in AAC60782. Ref.2
Sequence conflict72 – 8312AAGGS…LLSGG → RSRGKLVVALRW in AAC60782. Ref.2
Sequence conflict1261Missing in AAC60782. Ref.2
Sequence conflict129 – 1302QE → HQ in AAC60782. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q56878 [UniParc].

Last modified March 20, 2007. Version 3.
Checksum: E52BA3FD5A71ED61

FASTA55060,383
        10         20         30         40         50         60 
MRFSLSTTAA ALAVSLAFAP GWAVAWEKDK TYDITILHTN DHHGHFWQND HGEYGLAAQK 

        70         80         90        100        110        120 
TLVDDIRKQV AAAGGSLLLL SGGDINTGVP ESDLQDAEPD FRGMNLVGYD AMAIGNHEFD 

       130        140        150        160        170        180 
NPLSVLRQQE KWATFPLLSA NIYQKSTQQR LFKPYALFDK QGVKIAVIGL TTDDTAKIGN 

       190        200        210        220        230        240 
PEYFTDIEFR VPATEAKQVV EQLRKTEKPD IIIAATHMGH YDDGKHGSNA PGDVEMARSL 

       250        260        270        280        290        300 
PAGYLDMIVG GHSQDPVCMA SENHKQADYV PGTPCAPDRQ NGTWIVQAHE WGKYVGRADF 

       310        320        330        340        350        360 
KFRNGELKLV SYQLIPINLK KKVEKADGTS ERIFYTQEIA QDPSMLKLLT PFEQQGKAQL 

       370        380        390        400        410        420 
DVKVGSVNGK LEGDRSKVRF EQTNLARLLL AAQMERAGAD FAVMSGGGVR DSIDAGDITY 

       430        440        450        460        470        480 
KDVLKVQPFG NTLVYADMKG SEVEKYLAVV ANKKVDSGAY AQFANVSLVA DGKGVSNVKI 

       490        500        510        520        530        540 
QGKPLDPNKT YRLATLNFNA LGGDGYPKID TLPSYVNTGF IDAEVLKQYI EKHSPLDASQ 

       550 
YQPKGEIVYK 

« Hide

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. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 13174 / 8081.
[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

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL13101.1.
U46859 Genomic DNA. Translation: AAC60782.1. Different initiation.
RefSeqYP_001007248.1. NC_008800.1.

3D structure databases

ProteinModelPortalQ56878.
SMRQ56878. Positions 26-547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393305.YE3066.

Proteomic databases

PRIDEQ56878.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL13101; CAL13101; YE3066.
GeneID4714553.
KEGGyen:YE3066.
PATRIC18565839. VBIYerEnt11519_3261.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0737.
HOGENOMHOG000247216.
KOK11751.
OMAPFQDKGK.
OrthoDBEOG696BW0.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERPTHR11575. PTHR11575. 1 hit.
PfamPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR01607. APYRASEFAMLY.
SUPFAMSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUSHA_YERE8
AccessionPrimary (citable) accession number: Q56878
Secondary accession number(s): A1JN00
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 20, 2007
Last modified: June 11, 2014
This is version 99 of the entry and version 3 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