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 24-JAN-2024, entry version 86.
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.ENSBTAP00000062942; -.
DR PaxDb; 9913-ENSBTAP00000024072; -.
DR PeptideAtlas; Q3T063; -.
DR GeneID; 614254; -.
DR KEGG; bta:614254; -.
DR CTD; 23475; -.
DR eggNOG; KOG3008; Eukaryota.
DR InParanoid; Q3T063; -.
DR OrthoDB; 5473389at2759; -.
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; Aldolase class I; 1.
DR Gene3D; 3.90.1170.20; Quinolinate phosphoribosyl transferase, N-terminal domain; 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 NCBIfam; TIGR00078; nadC; 1.
DR PANTHER; PTHR32179; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE [CARBOXYLATING]; 1.
DR PANTHER; PTHR32179:SF3; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE [CARBOXYLATING]; 1.
DR Pfam; PF01729; QRPTase_C; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR PIRSF; PIRSF006250; NadC_ModD; 1.
DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 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
//
