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P07024

- USHA_ECOLI

UniProt

P07024 - USHA_ECOLI

Protein

Protein UshA

Gene

ushA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    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. 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: EcoCyc

    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

    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 – 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.
    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.
    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 156 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