ID   NUD22_RAT               Reviewed;         308 AA.
AC   Q6P9U1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary anterior lobe;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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 hydrolase family. {ECO:0000305}.
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DR   EMBL; BC060593; AAH60593.1; -; mRNA.
DR   RefSeq; NP_954521.1; NM_199090.2.
DR   RefSeq; XP_006230822.1; XM_006230760.3.
DR   AlphaFoldDB; Q6P9U1; -.
DR   SMR; Q6P9U1; -.
DR   STRING; 10116.ENSRNOP00000028734; -.
DR   iPTMnet; Q6P9U1; -.
DR   PhosphoSitePlus; Q6P9U1; -.
DR   PaxDb; Q6P9U1; -.
DR   Ensembl; ENSRNOT00000028734; ENSRNOP00000028734; ENSRNOG00000021158.
DR   GeneID; 293703; -.
DR   KEGG; rno:293703; -.
DR   UCSC; RGD:735224; rat.
DR   CTD; 84304; -.
DR   RGD; 735224; Nudt22.
DR   eggNOG; ENOG502QRSW; Eukaryota.
DR   GeneTree; ENSGT00390000017869; -.
DR   HOGENOM; CLU_061819_1_0_1; -.
DR   InParanoid; Q6P9U1; -.
DR   OMA; PEPQAVC; -.
DR   OrthoDB; 1587403at2759; -.
DR   PhylomeDB; Q6P9U1; -.
DR   TreeFam; TF106357; -.
DR   PRO; PR:Q6P9U1; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000021158; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q6P9U1; RN.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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..308
FT                   /note="Uridine diphosphate glucose pyrophosphatase NUDT22"
FT                   /id="PRO_0000263733"
FT   DOMAIN          117..284
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           174..195
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
SQ   SEQUENCE   308 AA;  33492 MW;  D1F5AFA138DB220C CRC64;
     MDPEVSLMLL CPPGGLSQEQ VSVELSPAHD RRPLPEGDKT ITAIWETRLQ AQPWIFDAPK
     FRLHSATLAS SSPEPQLLLH LGLTSYRDFL GTNWSSSASW LRQQGATDWG DKQAYLADPL
     GVGAALVTAD DFLVFLRRSQ QVAEAPGLVD VPGGHPEPQA LCSGSIPQHE DLPGELVVRE
     LFSSVLQEVC DEVNLPLHTL SQPLLLGIAC NETSAGRASA EFYVQCSLTS EEVRNYYLSG
     GPEANESTGI IFVETQRVQR LQETEMWAQL CPSAKGAILL YNRHPPLQSG AGKSHLSHPS
     VPALSLQL