NADC_RAT
ID NADC_RAT Reviewed; 299 AA.
AC Q5I0M2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 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=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).
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; BC088177; AAH88177.1; -; mRNA.
DR RefSeq; NP_001009646.1; NM_001009646.1.
DR AlphaFoldDB; Q5I0M2; -.
DR SMR; Q5I0M2; -.
DR STRING; 10116.ENSRNOP00000023080; -.
DR iPTMnet; Q5I0M2; -.
DR PhosphoSitePlus; Q5I0M2; -.
DR PaxDb; Q5I0M2; -.
DR PRIDE; Q5I0M2; -.
DR Ensembl; ENSRNOT00000023080; ENSRNOP00000023080; ENSRNOG00000016980.
DR GeneID; 293504; -.
DR KEGG; rno:293504; -.
DR UCSC; RGD:1310309; rat.
DR CTD; 23475; -.
DR RGD; 1310309; Qprt.
DR eggNOG; KOG3008; Eukaryota.
DR GeneTree; ENSGT00390000002761; -.
DR HOGENOM; CLU_039622_1_1_1; -.
DR InParanoid; Q5I0M2; -.
DR OMA; DMIMLKD; -.
DR OrthoDB; 1263431at2759; -.
DR PhylomeDB; Q5I0M2; -.
DR TreeFam; TF300845; -.
DR Reactome; R-RNO-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00331.
DR PRO; PR:Q5I0M2; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016980; Expressed in adult mammalian kidney and 17 other tissues.
DR Genevisible; Q5I0M2; RN.
DR GO; GO:1902494; C:catalytic complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IDA:RGD.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:RGD.
DR GO; GO:0034213; P:quinolinate catabolic process; ISO:RGD.
DR GO; GO:0046874; P:quinolinate metabolic process; IDA:RGD.
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; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..299
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000245464"
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"
SQ SEQUENCE 299 AA; 31297 MW; 7ADC91705C422FD3 CRC64;
MDPEGLQFLL PPASLAALAN SWLQEDCPGL NFASLVTGSA PAQAVLWAKS PGVLAGRPFF
DAIFTQLNCQ VSWLLPEGSK LVPVVKVAEV RGPAHHLLLG ERVALNTLAR CSGIASAAAT
AVEVATSTGW AGHVAGTRKT TPGFRLVEKY GLLVGGAECH RYDLGGLVMV KDNHVVAAGS
MEKAVLKARQ AAGFPLKVEV ECSSLKEALQ AAEAGADLVM LDNFKPEELH PTAATLKAKF
PNVSVEASGG VTLDNLPQFC GTNIDVISLG MLTQAAPALD FSLKLYAEGD IPVPHARRS
