ID A0A0D9R1A7_CHLSB Unreviewed; 299 AA.
AC A0A0D9R1A7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating] {ECO:0000256|ARBA:ARBA00020990, ECO:0000256|PIRNR:PIRNR006250};
DE EC=2.4.2.19 {ECO:0000256|ARBA:ARBA00011944, ECO:0000256|PIRNR:PIRNR006250};
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|ARBA:ARBA00033102, ECO:0000256|PIRNR:PIRNR006250};
GN Name=QPRT {ECO:0000313|Ensembl:ENSCSAP00000002396.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000002396.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000002396.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000002396.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000256|ARBA:ARBA00003237, ECO:0000256|PIRNR:PIRNR006250}.
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:0000256|ARBA:ARBA00000260,
CC ECO:0000256|PIRNR:PIRNR006250};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004893, ECO:0000256|PIRNR:PIRNR006250}.
CC -!- SUBUNIT: Hexamer formed by 3 homodimers.
CC {ECO:0000256|ARBA:ARBA00011218, ECO:0000256|PIRNR:PIRNR006250}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family.
CC {ECO:0000256|ARBA:ARBA00009400, ECO:0000256|PIRNR:PIRNR006250}.
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DR EMBL; AQIB01118707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01118708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01118709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01118710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01118711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01118712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007988132.1; XM_007989941.1.
DR AlphaFoldDB; A0A0D9R1A7; -.
DR STRING; 60711.ENSCSAP00000002396; -.
DR Ensembl; ENSCSAT00000004136.1; ENSCSAP00000002396.1; ENSCSAG00000006096.1.
DR GeneID; 103230847; -.
DR CTD; 23475; -.
DR eggNOG; KOG3008; Eukaryota.
DR GeneTree; ENSGT00390000002761; -.
DR OMA; DIVMCDN; -.
DR OrthoDB; 5473389at2759; -.
DR UniPathway; UPA00253; UER00331.
DR BioGRID-ORCS; 103230847; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 5.
DR Bgee; ENSCSAG00000006096; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:1902494; C:catalytic complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0034213; P:quinolinate catabolic process; IEA:Ensembl.
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 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|PIRNR:PIRNR006250};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|PIRNR:PIRNR006250};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..299
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002344218"
FT DOMAIN 34..112
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 114..284
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 137..139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 248..250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 269..271
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ SEQUENCE 299 AA; 31074 MW; CF78EA59F92D7A13 CRC64;
MDAEGLALLL PPVTLAALVD SWLREDCPGL NYAALVSGAG PSQAVLWAKS PGVLAGQPFF
DAIFTQLNCQ VSWFLPEGSK LVPVARVAEV RGPAHSLLLG ERVALNMLAR CSGIASAATA
AVEAARGAGW TGHVAGTRKT TPGFRLVEKY GLLVGGAASH RYDLGGLVMV KDNHVVAAGG
VEKAVRAARQ AADFALKVEV ECSSLQEAVQ AAEAGADLVL LDNFKPKELH PTAAALKAQF
PSVAVEASGG ITLDNLPQFC GPHIDVISMG MLTQAAPALD FSLKLFAKEA APVPKIHWS
//
