USHA_YERE8
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 03-AUG-2022, entry version 132.
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; Proteobacteria; 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 STRING; 393305.YE3066; -.
DR EnsemblBacteria; CAL13101; CAL13101; YE3066.
DR KEGG; yen:YE3066; -.
DR PATRIC; fig|393305.7.peg.3261; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_7_0_6; -.
DR OMA; VQPFTNM; -.
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 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 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
