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P07024

- USHA_ECOLI

UniProt

P07024 - USHA_ECOLI

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Protein
Protein UshA
Gene
ushA, b0480, JW0469
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Binds 2 zinc 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. UDP-sugar diphosphatase activity Source: EcoCyc
  3. metal ion binding Source: UniProtKB-KW
  4. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. nucleotide catabolic process Source: EcoCyc
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.
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11060. ushA.

Subcellular locationi

Periplasm
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 Publications
Add
BLAST
Chaini26 – 550525Protein UshA
PRO_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.

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP07024.
SMRiP07024. Positions 26-550.

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.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0737.
HOGENOMiHOG000247216.
KOiK11751.
OMAiNDTHSHL.
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

MKLLQRGVAL ALLTTFTLAS ETALAYEQDK TYKITVLHTN DHHGHFWRNE    50
YGEYGLAAQK TLVDGIRKEV AAEGGSVLLL SGGDINTGVP ESDLQDAEPD 100
FRGMNLVGYD AMAIGNHEFD NPLTVLRQQE KWAKFPLLSA NIYQKSTGER 150
LFKPWALFKR QDLKIAVIGL TTDDTAKIGN PEYFTDIEFR KPADEAKLVI 200
QELQQTEKPD IIIAATHMGH YDNGEHGSNA PGDVEMARAL PAGSLAMIVG 250
GHSQDPVCMA AENKKQVDYV PGTPCKPDQQ NGIWIVQAHE WGKYVGRADF 300
EFRNGEMKMV NYQLIPVNLK KKVTWEDGKS ERVLYTPEIA ENQQMISLLS 350
PFQNKGKAQL EVKIGETNGR LEGDRDKVRF VQTNMGRLIL AAQMDRTGAD 400
FAVMSGGGIR DSIEAGDISY KNVLKVQPFG NVVVYADMTG KEVIDYLTAV 450
AQMKPDSGAY PQFANVSFVA KDGKLNDLKI KGEPVDPAKT YRMATLNFNA 500
TGGDGYPRLD NKPGYVNTGF IDAEVLKAYI QKSSPLDVSV YEPKGEVSWQ 550
Length:550
Mass (Da):60,824
Last modified:November 1, 1997 - v2
Checksum:iDBA07B1C40C6C075
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561P → T in CAA27532. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
PIRi G64778. YXECUG.
RefSeqi NP_415013.1. NC_000913.3.
YP_488771.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HO5 X-ray 2.10 A/B 26-550 [» ]
1HP1 X-ray 1.70 A 26-541 [» ]
1HPU X-ray 1.85 A/B/C/D 26-550 [» ]
1OI8 X-ray 2.10 A/B 26-550 [» ]
1OID X-ray 2.10 A/B 26-550 [» ]
1OIE X-ray 2.33 A 26-550 [» ]
1USH X-ray 1.73 A 1-550 [» ]
2USH X-ray 2.22 A/B 1-550 [» ]
ProteinModelPortali P07024.
SMRi P07024. Positions 26-550.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-11096N.
IntActi P07024. 10 interactions.
MINTi MINT-1256646.
STRINGi 511145.b0480.

Proteomic databases

PaxDbi P07024.
PRIDEi P07024.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73582 ; AAC73582 ; b0480 .
BAE76259 ; BAE76259 ; BAE76259 .
GeneIDi 12930849.
947331.
KEGGi ecj:Y75_p0467.
eco:b0480.
PATRICi 32116117. VBIEscCol129921_0500.

Organism-specific databases

EchoBASEi EB1053.
EcoGenei EG11060. ushA.

Phylogenomic databases

eggNOGi COG0737.
HOGENOMi HOG000247216.
KOi K11751.
OMAi NDTHSHL.
OrthoDBi EOG696BW0.
PhylomeDBi P07024.

Enzyme and pathway databases

BioCyci EcoCyc:USHA-MONOMER.
ECOL316407:JW0469-MONOMER.
MetaCyc:USHA-MONOMER.
SABIO-RK P07024.

Miscellaneous databases

EvolutionaryTracei P07024.
PROi P07024.

Gene expression databases

Genevestigatori P07024.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProi IPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view ]
PANTHERi PTHR11575. PTHR11575. 1 hit.
Pfami PF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR01607. APYRASEFAMLY.
SUPFAMi SSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEi PS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 155 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

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