ID A0A1G4JWQ1_9SACH Unreviewed; 296 AA.
AC A0A1G4JWQ1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating] {ECO:0000256|PIRNR:PIRNR006250};
DE EC=2.4.2.19 {ECO:0000256|PIRNR:PIRNR006250};
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|PIRNR:PIRNR006250};
GN ORFNames=LADA_0G16138G {ECO:0000313|EMBL:SCU95538.1};
OS Lachancea dasiensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU95538.1, ECO:0000313|Proteomes:UP000190274};
RN [1] {ECO:0000313|Proteomes:UP000190274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {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|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|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; LT598457; SCU95538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4JWQ1; -.
DR STRING; 1266660.A0A1G4JWQ1; -.
DR OrthoDB; 5473389at2759; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000190274; Chromosome G.
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 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:UP000190274};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT DOMAIN 34..115
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 117..290
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
SQ SEQUENCE 296 AA; 32442 MW; 86E57CBBB7684DE2 CRC64;
MPQFEHLLPT NGDWKLDITR WLQEDVPSFD FGGFVVGSAA KSATLWMKEQ GVLSGIPFAQ
EVFDQCKLRV EWLVSEGSEL SPKKGEKIAI AKIHGEARNI LLAERTALNL LSRSSGIATA
SRNLINVARE VGYGGVIAGT RKTTPGLRRL EKYSMLVGGC DTHRYDLSSM VMLKDNHIWS
TGSITRAVED ARSVCGFAVK IEVECQSEAE ADEAILAGAD VIMLDNFSGQ TLQTAALNLK
QRWAGKKSFL LECSGGLKLS NIREYLCHDI DIYSTSSIHQ GTSVVDFSLK INVEGQ
//
