ID   NADC_BOVIN              Reviewed;         299 AA.
AC   Q3T063;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   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 (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC102550; AAI02551.1; -; mRNA.
DR   RefSeq; NP_001030523.1; NM_001035446.2.
DR   AlphaFoldDB; Q3T063; -.
DR   SMR; Q3T063; -.
DR   STRING; 9913.ENSBTAP00000024072; -.
DR   PaxDb; Q3T063; -.
DR   PeptideAtlas; Q3T063; -.
DR   PRIDE; Q3T063; -.
DR   GeneID; 614254; -.
DR   KEGG; bta:614254; -.
DR   CTD; 23475; -.
DR   eggNOG; KOG3008; Eukaryota.
DR   InParanoid; Q3T063; -.
DR   OrthoDB; 1263431at2759; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central.
DR   GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR   GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central.
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   2: Evidence at transcript 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_0000245463"
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:0000250|UniProtKB:Q91X91"
SQ   SEQUENCE   299 AA;  31151 MW;  B79ECAA600710728 CRC64;
     MDPEGLAHLL PPATLAALAD SWLREDCPGL NYVALVSGTA PSQAVLWAKS PGVLAGRPFL
     DAIFAQVNCQ VSWFLPEGSK LVPVAKVAEV RGPAHCLLLG ERVALNTLAR CSGVASMAAA
     AVETARGTGW AGHVAGTRKT TPGFRLVEKY GLLVGGAAAH RYDLGGLVMV KDNHVMAAGG
     VKKAVRAARR AADFALKVEV ECSSLQEAVE AAEAGADLVL LDNFRPEELH PTAATLKAQF
     PSVSVEASGG VRLDNLPQFC GPHIDVISLG MLTQAAPALD FSLKLFAEGA TPVPHARRS