ID   USHA_YERE8              Reviewed;         550 AA.
AC   Q56878; A1JN00;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 3.
DT   27-MAR-2024, entry version 139.
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; OrderedLocusNames=YE3066;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-374.
RA   Zhang L., Toivanen P., Skurnik M.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Note=Divalent metal cations. Most likely Co(2+). {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC60782.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM286415; CAL13101.1; -; Genomic_DNA.
DR   EMBL; U46859; AAC60782.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011816863.1; NC_008800.1.
DR   RefSeq; YP_001007248.1; NC_008800.1.
DR   AlphaFoldDB; Q56878; -.
DR   SMR; Q56878; -.
DR   KEGG; yen:YE3066; -.
DR   PATRIC; fig|393305.7.peg.3261; -.
DR   eggNOG; COG0737; Bacteria.
DR   HOGENOM; CLU_005854_7_0_6; -.
DR   OrthoDB; 9803927at2; -.
DR   Proteomes; UP000000642; Chromosome.
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   Cobalt; Disulfide bond; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Periplasm; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..550
FT                   /note="Protein UshA"
FT                   /id="PRO_0000000034"
FT   BINDING         41
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         375..379
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"
FT   CONFLICT        24
FT                   /note="V -> A (in Ref. 2; AAC60782)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="W -> C (in Ref. 2; AAC60782)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72..83
FT                   /note="AAGGSLLLLSGG -> RSRGKLVVALRW (in Ref. 2; AAC60782)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="Missing (in Ref. 2; AAC60782)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129..130
FT                   /note="QE -> HQ (in Ref. 2; AAC60782)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   550 AA;  60383 MW;  E52BA3FD5A71ED61 CRC64;
     MRFSLSTTAA ALAVSLAFAP GWAVAWEKDK TYDITILHTN DHHGHFWQND HGEYGLAAQK
     TLVDDIRKQV AAAGGSLLLL SGGDINTGVP ESDLQDAEPD FRGMNLVGYD AMAIGNHEFD
     NPLSVLRQQE KWATFPLLSA NIYQKSTQQR LFKPYALFDK QGVKIAVIGL TTDDTAKIGN
     PEYFTDIEFR VPATEAKQVV EQLRKTEKPD IIIAATHMGH YDDGKHGSNA PGDVEMARSL
     PAGYLDMIVG GHSQDPVCMA SENHKQADYV PGTPCAPDRQ NGTWIVQAHE WGKYVGRADF
     KFRNGELKLV SYQLIPINLK KKVEKADGTS ERIFYTQEIA QDPSMLKLLT PFEQQGKAQL
     DVKVGSVNGK LEGDRSKVRF EQTNLARLLL AAQMERAGAD FAVMSGGGVR DSIDAGDITY
     KDVLKVQPFG NTLVYADMKG SEVEKYLAVV ANKKVDSGAY AQFANVSLVA DGKGVSNVKI
     QGKPLDPNKT YRLATLNFNA LGGDGYPKID TLPSYVNTGF IDAEVLKQYI EKHSPLDASQ
     YQPKGEIVYK
//