ID G3T517_LOXAF Unreviewed; 299 AA.
AC G3T517;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:ENSLAFP00000008492.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000008492.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000008492.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008492.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000008492.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008492.3};
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 AlphaFoldDB; G3T517; -.
DR STRING; 9785.ENSLAFP00000008492; -.
DR Ensembl; ENSLAFT00000010132.3; ENSLAFP00000008492.3; ENSLAFG00000010134.3.
DR eggNOG; KOG3008; Eukaryota.
DR GeneTree; ENSGT00390000002761; -.
DR HOGENOM; CLU_039622_1_1_1; -.
DR InParanoid; G3T517; -.
DR OMA; DIVMCDN; -.
DR TreeFam; TF300845; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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:UP000007646};
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_5003454730"
FT DOMAIN 33..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; 31006 MW; 8C5CDED533BD8A6E CRC64;
WDPQNLALLL PPTTLAALAG AWLQEDCPGL NYTALVTGAA PSQAALWAKS PGVLAGRPFF
DAIFAQLNCQ VSWYLPEGSK LVPVAKVAEV RGPAHCLLLG ERVALNTLAR CSGVASAAAY
AVEAARGTGW TGCVAGTRKT TPGFRLVEKY GLLVGGAASH RYDLGGLVMV KDNHIVAAGS
VEKAVRGAQR AANFALKVEV ECSSLQEAVE AAQAGADLVL LDNFMPEELH PTAAALKAQF
PSVGVEASGG ITLGNLPQFC GPHIDVISLG MLTQAAQALD FSLKVFAEGA TPVPHTRQS
//