ID   NUD22_BOVIN             Reviewed;         290 AA.
AC   Q2TBI8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Uridine diphosphate glucose pyrophosphatase NUDT22;
DE            Short=UDPG pyrophosphatase;
DE            Short=UGPPase;
DE            EC=3.6.1.45;
DE   AltName: Full=Nucleoside diphosphate-linked moiety X motif 22;
DE            Short=Nudix motif 22;
GN   Name=NUDT22;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and
CC       UDP-galactose to galactose 1-phosphate and UMP. Preferred substrate is
CC       UDP-glucose. {ECO:0000250|UniProtKB:Q9BRQ3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.;
CC         EC=3.6.1.45; Evidence={ECO:0000250|UniProtKB:Q9BRQ3};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9BRQ3};
CC   -!- SIMILARITY: Belongs to the Nudix family. {ECO:0000305}.
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DR   EMBL; BC110129; AAI10130.1; -; mRNA.
DR   RefSeq; NP_001033769.1; NM_001038680.1.
DR   AlphaFoldDB; Q2TBI8; -.
DR   SMR; Q2TBI8; -.
DR   STRING; 9913.ENSBTAP00000043364; -.
DR   PaxDb; Q2TBI8; -.
DR   GeneID; 533578; -.
DR   KEGG; bta:533578; -.
DR   CTD; 84304; -.
DR   eggNOG; ENOG502QRSW; Eukaryota.
DR   HOGENOM; CLU_061819_1_0_1; -.
DR   InParanoid; Q2TBI8; -.
DR   OrthoDB; 1587403at2759; -.
DR   TreeFam; TF106357; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0052751; F:GDP-mannose hydrolase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR   GO; GO:0008768; F:UDP-sugar diphosphatase activity; ISS:UniProtKB.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PROSITE; PS51462; NUDIX; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..290
FT                   /note="Uridine diphosphate glucose pyrophosphatase NUDT22"
FT                   /id="PRO_0000263730"
FT   DOMAIN          118..285
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           175..196
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         189
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
SQ   SEQUENCE   290 AA;  31419 MW;  CC08A92F0A33D044 CRC64;
     MDPEVSLLLQ CPPGGLPEKQ VRAELSPAYD RRPLPGGDKA IIAIWESRLQ AQPWLFNAPK
     FRLHSATLAP TGLPGPQLLL RLGLTSYQDF LGTNWASSAA WLRQQGATDW GDKQAYLADP
     LGVGAALATA DDFLVFLRRS GQVAEAPGLV DVPGGHPEPQ ALCPGDSPLH KDLPGELVVH
     ELFSSVLQEI CDEVNVPPLT LSQPLLLGIA CNETSAGRAS AEFYVQCSLT SEQVRRHYMS
     GGPEAHESTG IIFVEKQSMQ RLQETEMWPE LCPSAKGAIF LYNRVQGSST