ID   NADC_HELPJ              Reviewed;         273 AA.
AC   Q9ZJN2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE            EC=2.4.2.19;
DE   AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE            Short=QAPRTase;
GN   Name=nadC; OrderedLocusNames=jhp_1273;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC       {ECO:0000250}.
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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from quinolinate: step 1/1.
CC   -!- SUBUNIT: Hexamer formed by 3 homodimers. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD06845.1; -; Genomic_DNA.
DR   PIR; H71827; H71827.
DR   RefSeq; WP_000404063.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZJN2; -.
DR   SMR; Q9ZJN2; -.
DR   STRING; 85963.jhp_1273; -.
DR   PRIDE; Q9ZJN2; -.
DR   EnsemblBacteria; AAD06845; AAD06845; jhp_1273.
DR   KEGG; hpj:jhp_1273; -.
DR   PATRIC; fig|85963.30.peg.1296; -.
DR   eggNOG; COG0157; Bacteria.
DR   OMA; DMIMLKD; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000000804; Chromosome.
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; -; 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   3: Inferred from homology;
KW   Glycosyltransferase; Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN           1..273
FT                   /note="Probable nicotinate-nucleotide pyrophosphorylase
FT                   [carboxylating]"
FT                   /id="PRO_0000155944"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         124..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         235..237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         256..258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   273 AA;  30659 MW;  1F7EC956673A7BA4 CRC64;
     MEIKTFLECA LKEDLGHGDL FERVLEKDFK ATAFVRAKQE GVFSGEKYAL ELLQMTGIEC
     VQNIKDKERF KPKDTLMEIR GDFSMLLKIE RTLLNLLQHS SGIATLTSRF VEALNSPKVR
     LLDTRKTRPL LRIFEKYSVL NGGASNHRLG LDDALMLKDT HLKHVKDLKS FLTHARKNLP
     FTAKIEIECE SFEEAKNAMS AGADIVMCDN MSVGETKEIA AYREAHYPFV LLEASGNISL
     ESINAYAKSG VDAISVGALI HQATFIDMHM KMA