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Protein

Protein UshA

Gene

ushA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.
A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi41 – 411Zinc 1
Metal bindingi43 – 431Zinc 1
Metal bindingi84 – 841Zinc 1
Metal bindingi84 – 841Zinc 2
Metal bindingi116 – 1161Zinc 2
Sitei117 – 1171Transition state stabilizer
Sitei120 – 1201Transition state stabilizer
Metal bindingi217 – 2171Zinc 2
Metal bindingi252 – 2521Zinc 2
Metal bindingi254 – 2541Zinc 1

GO - Molecular functioni

  1. 5'-nucleotidase activity Source: EcoCyc
  2. metal ion binding Source: UniProtKB-KW
  3. nucleotide binding Source: UniProtKB-KW
  4. UDP-sugar diphosphatase activity Source: EcoCyc

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. nucleotide catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:USHA-MONOMER.
ECOL316407:JW0469-MONOMER.
MetaCyc:USHA-MONOMER.
BRENDAi3.1.3.5. 2026.
SABIO-RKP07024.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein UshA
Including the following 2 domains:
UDP-sugar hydrolase (EC:3.6.1.45)
Alternative name(s):
UDP-sugar diphosphatase
UDP-sugar pyrophosphatase
5'-nucleotidase (EC:3.1.3.5)
Short name:
5'-NT
Gene namesi
Name:ushA
Ordered Locus Names:b0480, JW0469
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11060. ushA.

Subcellular locationi

  1. Periplasm

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

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25252 PublicationsAdd
BLAST
Chaini26 – 550525Protein UshAPRO_0000000031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi258 ↔ 275

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP07024.
PRIDEiP07024.

Expressioni

Gene expression databases

GenevestigatoriP07024.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

DIPiDIP-11096N.
IntActiP07024. 10 interactions.
MINTiMINT-1256646.
STRINGi511145.b0480.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 398Combined sources
Helixi56 – 7318Combined sources
Beta strandi76 – 816Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 934Combined sources
Turni94 – 974Combined sources
Helixi98 – 10710Combined sources
Beta strandi111 – 1133Combined sources
Helixi116 – 1194Combined sources
Helixi123 – 13210Combined sources
Beta strandi140 – 1445Combined sources
Turni145 – 1473Combined sources
Beta strandi150 – 16011Combined sources
Beta strandi163 – 1719Combined sources
Turni173 – 1775Combined sources
Beta strandi178 – 1803Combined sources
Helixi181 – 1844Combined sources
Beta strandi187 – 1893Combined sources
Helixi192 – 20615Combined sources
Beta strandi210 – 2189Combined sources
Helixi222 – 2243Combined sources
Helixi233 – 2397Combined sources
Beta strandi244 – 2496Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi283 – 2864Combined sources
Beta strandi293 – 30311Combined sources
Beta strandi306 – 31813Combined sources
Beta strandi320 – 3245Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi333 – 3364Combined sources
Helixi343 – 35917Combined sources
Beta strandi362 – 3698Combined sources
Helixi375 – 3784Combined sources
Helixi384 – 39714Combined sources
Beta strandi400 – 4056Combined sources
Helixi406 – 4083Combined sources
Beta strandi415 – 4195Combined sources
Helixi420 – 4267Combined sources
Beta strandi432 – 4398Combined sources
Helixi440 – 45011Combined sources
Beta strandi455 – 4573Combined sources
Beta strandi461 – 47111Combined sources
Beta strandi474 – 4807Combined sources
Beta strandi489 – 4968Combined sources
Helixi497 – 5004Combined sources
Helixi503 – 5053Combined sources
Beta strandi512 – 5143Combined sources
Beta strandi515 – 5217Combined sources
Helixi522 – 53312Combined sources
Helixi538 – 5414Combined sources
Beta strandi545 – 5506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HO5X-ray2.10A/B26-550[»]
1HP1X-ray1.70A26-541[»]
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[»]
4WWLX-ray2.23A26-550[»]
ProteinModelPortaliP07024.
SMRiP07024. Positions 26-550.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07024.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni375 – 3795Substrate binding
Regioni498 – 5047Substrate binding

Sequence similaritiesi

Belongs to the 5'-nucleotidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0737.
HOGENOMiHOG000247216.
InParanoidiP07024.
KOiK11751.
OMAiTLNILHI.
OrthoDBiEOG696BW0.
PhylomeDBiP07024.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLQRGVAL ALLTTFTLAS ETALAYEQDK TYKITVLHTN DHHGHFWRNE
60 70 80 90 100
YGEYGLAAQK TLVDGIRKEV AAEGGSVLLL SGGDINTGVP ESDLQDAEPD
110 120 130 140 150
FRGMNLVGYD AMAIGNHEFD NPLTVLRQQE KWAKFPLLSA NIYQKSTGER
160 170 180 190 200
LFKPWALFKR QDLKIAVIGL TTDDTAKIGN PEYFTDIEFR KPADEAKLVI
210 220 230 240 250
QELQQTEKPD IIIAATHMGH YDNGEHGSNA PGDVEMARAL PAGSLAMIVG
260 270 280 290 300
GHSQDPVCMA AENKKQVDYV PGTPCKPDQQ NGIWIVQAHE WGKYVGRADF
310 320 330 340 350
EFRNGEMKMV NYQLIPVNLK KKVTWEDGKS ERVLYTPEIA ENQQMISLLS
360 370 380 390 400
PFQNKGKAQL EVKIGETNGR LEGDRDKVRF VQTNMGRLIL AAQMDRTGAD
410 420 430 440 450
FAVMSGGGIR DSIEAGDISY KNVLKVQPFG NVVVYADMTG KEVIDYLTAV
460 470 480 490 500
AQMKPDSGAY PQFANVSFVA KDGKLNDLKI KGEPVDPAKT YRMATLNFNA
510 520 530 540 550
TGGDGYPRLD NKPGYVNTGF IDAEVLKAYI QKSSPLDVSV YEPKGEVSWQ
Length:550
Mass (Da):60,824
Last modified:November 1, 1997 - v2
Checksum:iDBA07B1C40C6C075
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561P → T in CAA27532 (PubMed:3012467).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiG64778. YXECUG.
RefSeqiNP_415013.1. NC_000913.3.
YP_488771.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73582; AAC73582; b0480.
BAE76259; BAE76259; BAE76259.
GeneIDi12930849.
947331.
KEGGiecj:Y75_p0467.
eco:b0480.
PATRICi32116117. VBIEscCol129921_0500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiG64778. YXECUG.
RefSeqiNP_415013.1. NC_000913.3.
YP_488771.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HO5X-ray2.10A/B26-550[»]
1HP1X-ray1.70A26-541[»]
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[»]
4WWLX-ray2.23A26-550[»]
ProteinModelPortaliP07024.
SMRiP07024. Positions 26-550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-11096N.
IntActiP07024. 10 interactions.
MINTiMINT-1256646.
STRINGi511145.b0480.

Proteomic databases

PaxDbiP07024.
PRIDEiP07024.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73582; AAC73582; b0480.
BAE76259; BAE76259; BAE76259.
GeneIDi12930849.
947331.
KEGGiecj:Y75_p0467.
eco:b0480.
PATRICi32116117. VBIEscCol129921_0500.

Organism-specific databases

EchoBASEiEB1053.
EcoGeneiEG11060. ushA.

Phylogenomic databases

eggNOGiCOG0737.
HOGENOMiHOG000247216.
InParanoidiP07024.
KOiK11751.
OMAiTLNILHI.
OrthoDBiEOG696BW0.
PhylomeDBiP07024.

Enzyme and pathway databases

BioCyciEcoCyc:USHA-MONOMER.
ECOL316407:JW0469-MONOMER.
MetaCyc:USHA-MONOMER.
BRENDAi3.1.3.5. 2026.
SABIO-RKP07024.

Miscellaneous databases

EvolutionaryTraceiP07024.
PROiP07024.

Gene expression databases

GenevestigatoriP07024.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiUSHA_ECOLI
AccessioniPrimary (citable) accession number: P07024
Secondary accession number(s): P78274, Q2MBU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: April 1, 2015
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.