USHA_SALPU
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-AUG-2022, entry version 93.
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; Proteobacteria; 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 Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 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; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 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
