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P07024 (USHA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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:b0480, JW0469
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell.

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.

Enzyme regulation

The activity of this protein is inhibited by an intracellular protein inhibitor.

Subunit structure

Monomer.

Subcellular location

Periplasm. Note: Exported from the cell, except a small proportion that is internally localized.

Sequence similarities

Belongs to the 5'-nucleotidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.1 Ref.6
Chain26 – 550525Protein UshA
PRO_0000000031

Regions

Region375 – 3795Substrate binding
Region498 – 5047Substrate binding

Sites

Metal binding411Zinc 1
Metal binding431Zinc 1
Metal binding841Zinc 1
Metal binding841Zinc 2
Metal binding1161Zinc 2
Metal binding2171Zinc 2
Metal binding2521Zinc 2
Metal binding2541Zinc 1
Site1171Transition state stabilizer
Site1201Transition state stabilizer

Amino acid modifications

Disulfide bond258 ↔ 275

Experimental info

Sequence conflict2561P → T in CAA27532. Ref.1

Secondary structure

1 ............................................................................................. 550
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07024 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: DBA07B1C40C6C075

FASTA55060,824
        10         20         30         40         50         60 
MKLLQRGVAL ALLTTFTLAS ETALAYEQDK TYKITVLHTN DHHGHFWRNE YGEYGLAAQK 

        70         80         90        100        110        120 
TLVDGIRKEV AAEGGSVLLL SGGDINTGVP ESDLQDAEPD FRGMNLVGYD AMAIGNHEFD 

       130        140        150        160        170        180 
NPLTVLRQQE KWAKFPLLSA NIYQKSTGER LFKPWALFKR QDLKIAVIGL TTDDTAKIGN 

       190        200        210        220        230        240 
PEYFTDIEFR KPADEAKLVI QELQQTEKPD IIIAATHMGH YDNGEHGSNA PGDVEMARAL 

       250        260        270        280        290        300 
PAGSLAMIVG GHSQDPVCMA AENKKQVDYV PGTPCKPDQQ NGIWIVQAHE WGKYVGRADF 

       310        320        330        340        350        360 
EFRNGEMKMV NYQLIPVNLK KKVTWEDGKS ERVLYTPEIA ENQQMISLLS PFQNKGKAQL 

       370        380        390        400        410        420 
EVKIGETNGR LEGDRDKVRF VQTNMGRLIL AAQMDRTGAD FAVMSGGGIR DSIEAGDISY 

       430        440        450        460        470        480 
KNVLKVQPFG NVVVYADMTG KEVIDYLTAV AQMKPDSGAY PQFANVSFVA KDGKLNDLKI 

       490        500        510        520        530        540 
KGEPVDPAKT YRMATLNFNA TGGDGYPRLD NKPGYVNTGF IDAEVLKAYI QKSSPLDVSV 

       550 
YEPKGEVSWQ

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and transcriptional analysis of the E. coli ushA gene, encoding periplasmic UDP-sugar hydrolase (5'-nucleotidase): regulation of the ushA gene, and the signal sequence of its encoded protein product."
Burns D.M., Beacham I.R.
Nucleic Acids Res. 14:4325-4342(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-27.
[2]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]Fujisaki S., Ohnuma S., Horiuchi T., Takahashi I., Tsukui S., Nishimura Y., Nishino T., Inokuchi H.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
Strain: K12 / DH5-alpha.
[6]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-37.
Strain: K12 / EMG2.
[7]"X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site."
Knoefel T., Straeter N.
Nat. Struct. Biol. 6:448-453(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 26-550.
[8]"Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures."
Knoefel T., Straeter N.
J. Mol. Biol. 309:239-254(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; PRODUCT AND INHIBITOR.
[9]"E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion."
Knoefel T., Straeter N.
J. Mol. Biol. 309:255-266(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X03895 Genomic DNA. Translation: CAA27532.1.
U82664 Genomic DNA. Translation: AAB40234.1.
U00096 Genomic DNA. Translation: AAC73582.1.
AP009048 Genomic DNA. Translation: BAE76259.1.
D73370 Genomic DNA. No translation available.
PIRYXECUG. G64778.
RefSeqNP_415013.1. NC_000913.2.
YP_488771.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HO5X-ray2.10A/B26-550[»]
1HP1X-ray1.70A26-550[»]
1HPUX-ray1.85A/B/C/D26-550[»]
1OI8X-ray2.10A/B26-550[»]
1OIDX-ray2.10A/B26-550[»]
1OIEX-ray2.33A26-550[»]
1USHX-ray1.73A1-550[»]
2USHX-ray2.22A/B1-550[»]
ProteinModelPortalP07024.
SMRP07024. Positions 26-550.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-11096N.
IntActP07024. 10 interactions.
MINTMINT-1256646.
STRING511145.b0480.

Proteomic databases

PaxDbP07024.
PRIDEP07024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73582; AAC73582; b0480.
BAE76259; BAE76259; BAE76259.
GeneID12930849.
947331.
KEGGecj:Y75_p0467.
eco:b0480.
PATRIC32116117. VBIEscCol129921_0500.

Organism-specific databases

EchoBASEEB1053.
EcoGeneEG11060. ushA.

Phylogenomic databases

eggNOGCOG0737.
HOGENOMHOG000247216.
KOK11751.
OMAESGKDTQ.
ProtClustDBPRK09558.

Enzyme and pathway databases

BioCycEcoCyc:USHA-MONOMER.
ECOL316407:JW0469-MONOMER.
MetaCyc:USHA-MONOMER.
SABIO-RKP07024.

Gene expression databases

GenevestigatorP07024.

Family and domain databases

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

Other

EvolutionaryTraceP07024.

Entry information

Entry nameUSHA_ECOLI
AccessionPrimary (citable) accession number: P07024
Secondary accession number(s): P78274, Q2MBU7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents