ID H1S277_9BURK Unreviewed; 298 AA.
AC H1S277;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=nicotinate-nucleotide diphosphorylase (carboxylating) {ECO:0000256|ARBA:ARBA00011944};
DE EC=2.4.2.19 {ECO:0000256|ARBA:ARBA00011944};
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|ARBA:ARBA00033102};
GN ORFNames=OR16_08969 {ECO:0000313|EMBL:EHP43279.1};
OS Cupriavidus basilensis OR16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP43279.1, ECO:0000313|Proteomes:UP000005808};
RN [1] {ECO:0000313|EMBL:EHP43279.1, ECO:0000313|Proteomes:UP000005808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:EHP43279.1,
RC ECO:0000313|Proteomes:UP000005808};
RX PubMed=22461549; DOI=10.1128/JB.06752-11;
RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA Nagy I., Horvath B., Nagy I., Kukolya J.;
RT "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL J. Bacteriol. 194:2109-2110(2012).
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000256|ARBA:ARBA00003237}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004893}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family.
CC {ECO:0000256|ARBA:ARBA00009400, ECO:0000256|PIRNR:PIRNR006250}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHP43279.1}.
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DR EMBL; AHJE01000020; EHP43279.1; -; Genomic_DNA.
DR RefSeq; WP_006157510.1; NZ_AHJE01000020.1.
DR AlphaFoldDB; H1S277; -.
DR PATRIC; fig|1127483.3.peg.1793; -.
DR OrthoDB; 9782546at2; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000005808; Unassembled WGS sequence.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT DOMAIN 41..129
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 131..295
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 152..154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 259..261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 280..282
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ SEQUENCE 298 AA; 31369 MW; 9058A2CC41296F47 CRC64;
MSSNPNVNTV NSSRNAIFDS YGPALAEALL ANVGAAIAED VGSGDLTGLL VPVGKPARAR
VIVREQAVLC GQPWFEACMR AVDPALQVVW RQAEGARMAP DSVVCEITGP ARSLLTAERP
SLNFLQLLSG VATATRRYAD LVEGTSARVL DTRKTLPGLR LAQKYAVRVG GGDNQRLALY
DGILIKENHI AAAGSITAAM QAAAALDAGV SVQVEVENLA ELEEALAAGA KSILIDNFTE
TMMRDAVRIN AGRALLEVSG GVNADTIRVF AETGVDRISV GALTKDVRAT DYSLRIIE
//
