ID   NADC_MOUSE              Reviewed;         299 AA.
AC   Q91X91;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE            EC=2.4.2.19;
DE   AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE            Short=QAPRTase;
DE            Short=QPRTase;
GN   Name=Qprt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-291, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC       {ECO:0000250|UniProtKB:Q15274}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate;
CC         Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC         ChEBI:CHEBI:58017; EC=2.4.2.19;
CC         Evidence={ECO:0000250|UniProtKB:Q15274};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from quinolinate: step 1/1.
CC       {ECO:0000250|UniProtKB:Q15274}.
CC   -!- SUBUNIT: Hexamer formed by 3 homodimers.
CC       {ECO:0000250|UniProtKB:Q15274}.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR   EMBL; BC011191; AAH11191.1; -; mRNA.
DR   CCDS; CCDS40138.1; -.
DR   RefSeq; NP_598447.1; NM_133686.1.
DR   AlphaFoldDB; Q91X91; -.
DR   SMR; Q91X91; -.
DR   BioGRID; 212144; 1.
DR   IntAct; Q91X91; 1.
DR   MINT; Q91X91; -.
DR   STRING; 10090.ENSMUSP00000032912; -.
DR   iPTMnet; Q91X91; -.
DR   PhosphoSitePlus; Q91X91; -.
DR   SwissPalm; Q91X91; -.
DR   jPOST; Q91X91; -.
DR   MaxQB; Q91X91; -.
DR   PaxDb; Q91X91; -.
DR   PeptideAtlas; Q91X91; -.
DR   PRIDE; Q91X91; -.
DR   ProteomicsDB; 287346; -.
DR   Antibodypedia; 26777; 334 antibodies from 26 providers.
DR   DNASU; 67375; -.
DR   Ensembl; ENSMUST00000032912; ENSMUSP00000032912; ENSMUSG00000030674.
DR   GeneID; 67375; -.
DR   KEGG; mmu:67375; -.
DR   UCSC; uc009jug.1; mouse.
DR   CTD; 23475; -.
DR   MGI; MGI:1914625; Qprt.
DR   VEuPathDB; HostDB:ENSMUSG00000030674; -.
DR   eggNOG; KOG3008; Eukaryota.
DR   GeneTree; ENSGT00390000002761; -.
DR   HOGENOM; CLU_039622_1_1_1; -.
DR   InParanoid; Q91X91; -.
DR   OMA; DMIMLKD; -.
DR   OrthoDB; 1263431at2759; -.
DR   PhylomeDB; Q91X91; -.
DR   TreeFam; TF300845; -.
DR   Reactome; R-MMU-196807; Nicotinate metabolism.
DR   UniPathway; UPA00253; UER00331.
DR   BioGRID-ORCS; 67375; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q91X91; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q91X91; protein.
DR   Bgee; ENSMUSG00000030674; Expressed in left lobe of liver and 89 other tissues.
DR   Genevisible; Q91X91; MM.
DR   GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; ISO:MGI.
DR   GO; GO:0009435; P:NAD biosynthetic process; ISO:MGI.
DR   GO; GO:0034213; P:quinolinate catabolic process; ISO:MGI.
DR   GO; GO:0046874; P:quinolinate metabolic process; ISO:MGI.
DR   CDD; cd01572; QPRTase; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.90.1170.20; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004393; NadC.
DR   InterPro; IPR027277; NadC/ModD.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR   PANTHER; PTHR32179; PTHR32179; 1.
DR   Pfam; PF01729; QRPTase_C; 1.
DR   Pfam; PF02749; QRPTase_N; 1.
DR   PIRSF; PIRSF006250; NadC_ModD; 1.
DR   SUPFAM; SSF51690; SSF51690; 1.
DR   TIGRFAMs; TIGR00078; nadC; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..299
FT                   /note="Nicotinate-nucleotide pyrophosphorylase
FT                   [carboxylating]"
FT                   /id="PRO_0000155955"
FT   REGION          8..12
FT                   /note="Important for hexamer formation"
FT                   /evidence="ECO:0000250|UniProtKB:Q15274"
FT   BINDING         102
FT                   /ligand="quinolinate"
FT                   /ligand_id="ChEBI:CHEBI:29959"
FT                   /evidence="ECO:0000250|UniProtKB:Q15274"
FT   BINDING         138..139
FT                   /ligand="quinolinate"
FT                   /ligand_id="ChEBI:CHEBI:29959"
FT                   /evidence="ECO:0000250|UniProtKB:Q15274"
FT   BINDING         160..161
FT                   /ligand="quinolinate"
FT                   /ligand_id="ChEBI:CHEBI:29959"
FT                   /evidence="ECO:0000250|UniProtKB:Q15274"
FT   BINDING         171
FT                   /ligand="quinolinate"
FT                   /ligand_id="ChEBI:CHEBI:29959"
FT                   /evidence="ECO:0000250|UniProtKB:Q15274"
FT   BINDING         201
FT                   /ligand="quinolinate"
FT                   /ligand_id="ChEBI:CHEBI:29959"
FT                   /evidence="ECO:0000250|UniProtKB:Q15274"
FT   BINDING         222
FT                   /ligand="quinolinate"
FT                   /ligand_id="ChEBI:CHEBI:29959"
FT                   /evidence="ECO:0000250|UniProtKB:Q15274"
FT   BINDING         248..250
FT                   /ligand="quinolinate"
FT                   /ligand_id="ChEBI:CHEBI:29959"
FT                   /evidence="ECO:0000250|UniProtKB:Q15274"
FT   BINDING         270
FT                   /ligand="quinolinate"
FT                   /ligand_id="ChEBI:CHEBI:29959"
FT                   /evidence="ECO:0000250|UniProtKB:Q15274"
FT   MOD_RES         291
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   299 AA;  31530 MW;  4CF7FD0E6E290AAF CRC64;
     MDPEGLQLLL PPTTLAALAN SWLQEDCPGL NFASLVTGSA PSQAVLWAKS PGVLAGRPFF
     DAIFTQLNCQ VSWFLPEGSK LVPVVKVAEV KGPAHHLLLG ERVALNTLAR CSGIASAAAT
     AVEVARSTGW TGHVAGTRKT TPGFRLVEKY GLQVGGAACH RYDLGGMVMV KDNHVVAAGS
     MERAVLKARQ AAGFSLKVEV ECSSLEEAFR AAEAGADLVM LDNFKPEELH PTAATLKARF
     PSVSVEASGG VTLDNLTQFC GTHIDVISLG MLTQAAPALD FSLKLFAEGD TPVPHARRF