ID USHA_SALPU Reviewed; 550 AA. AC Q9RN37; DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 03-MAY-2023, entry version 96. DE RecName: Full=Protein UshA; DE Includes: DE RecName: Full=UDP-sugar hydrolase; DE EC=3.6.1.45; DE AltName: Full=UDP-sugar diphosphatase; DE AltName: Full=UDP-sugar pyrophosphatase; DE Includes: DE RecName: Full=5'-nucleotidase; DE Short=5'-NT; DE EC=3.1.3.5; DE Flags: Precursor; GN Name=ushA; OS Salmonella pullorum. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=605; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11429465; DOI=10.1099/00221287-147-7-1887; RA Innes D., Beacham I.R., Beven C.-A., Douglas M., Laird M.W., Joly J.C., RA Burns D.M.; RT "The cryptic ushA gene (ushA(c)) in natural isolates of Salmonella enterica RT (serotype Typhimurium) has been inactivated by a single missense RT mutation."; RL Microbiology 147:1887-1896(2001). CC -!- FUNCTION: Degradation of external UDP-glucose to uridine monophosphate CC and glucose-1-phosphate, which can then be used by the cell. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.; CC EC=3.6.1.45; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF188727; AAF05581.1; -; Genomic_DNA. DR AlphaFoldDB; Q9RN37; -. DR SMR; Q9RN37; -. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC. DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro. DR CDD; cd07405; MPP_UshA_N; 1. DR Gene3D; 3.60.21.10; -; 1. DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR036907; 5'-Nucleotdase_C_sf. DR InterPro; IPR006146; 5'-Nucleotdase_CS. DR InterPro; IPR006179; 5_nucleotidase/apyrase. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1. DR PANTHER; PTHR11575:SF46; PROTEIN USHA; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. PE 3: Inferred from homology; KW Disulfide bond; Hydrolase; Metal-binding; Nucleotide-binding; Periplasm; KW Signal; Zinc. FT SIGNAL 1..25 FT /evidence="ECO:0000250" FT CHAIN 26..550 FT /note="Protein UshA" FT /id="PRO_0000000032" FT BINDING 41 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 43 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 116 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 217 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 254 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 429 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 498..504 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 117 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT SITE 120 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT DISULFID 258..275 FT /evidence="ECO:0000250" SQ SEQUENCE 550 AA; 60604 MW; 655BC7E8F0D4F62F CRC64; MKFLKRGVAL ALLAAFALTT QPAQAYEKDK TYKITILHTN DHHGHFWRSE YGEYGLAAQK TLVDSIRKEV AQEGGGVLLL SGGDINTGVP ESDLQDAEPD FRGMNLIGYD AMAVGNHEFD NPLTVLRQQE KWAKFPFLSA NIYQKSTGER LFKPWAIFTR QDIKIAVIGL TTDDTAKIGN PEYFTDIEFR KPAEEAKVVI QELNMNEKPD VIIATTHMGH YDNGDHGSNA PGDVEMARSL PAGSLAMIVG GHSQDPVCMA SENKKQVNYV PGTPCAPDKQ NGIWIVQAHE WGKYVGRADF EFRNGEMKMV NYQLIPVNLK KKVTWDNGKS ERVLYTPEIA ENPQMLLLLT PFQNKGKVQL EVKIGSVNGL LEGDRSKVRF VQTNMGRVIL AAQIARTGAD FGVMSGGGIR DSIEAGDITY KSVLKVQPFG NIVVYADMSG KEVVDYLTRV AQMKPDSGAY PQLANVSFVA KEGKLTDLKI KGEPVDPAKT YRMATLSFNA TGGDGYPRID NKPGYVNTGF IDAEVLKEFI QQNSPLDAAA FTPKGEVSWL //