ID NADC_HELPY Reviewed; 273 AA. AC O25909; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 133. 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=HP_1355; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND RP SUBUNIT. RX PubMed=16419067; DOI=10.1002/prot.20834; RA Kim M.-K., Im Y.J., Lee J.H., Eom S.H.; RT "Crystal structure of quinolinic acid phosphoribosyltransferase from RT Helicobacter pylori."; RL Proteins 63:252-255(2006). 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:0000269|PubMed:16419067}. CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000511; AAD08397.1; -; Genomic_DNA. DR PIR; C64689; C64689. DR RefSeq; NP_208147.1; NC_000915.1. DR RefSeq; WP_000405980.1; NC_018939.1. DR PDB; 2B7N; X-ray; 2.30 A; A/B/C=1-273. DR PDB; 2B7P; X-ray; 2.51 A; A/B/C=1-273. DR PDB; 2B7Q; X-ray; 3.31 A; A/B/C=1-273. DR PDBsum; 2B7N; -. DR PDBsum; 2B7P; -. DR PDBsum; 2B7Q; -. DR AlphaFoldDB; O25909; -. DR SMR; O25909; -. DR DIP; DIP-3329N; -. DR IntAct; O25909; 3. DR MINT; O25909; -. DR STRING; 85962.HP_1355; -. DR PaxDb; 85962-C694_06995; -. DR EnsemblBacteria; AAD08397; AAD08397; HP_1355. DR KEGG; hpy:HP_1355; -. DR PATRIC; fig|85962.47.peg.1451; -. DR eggNOG; COG0157; Bacteria. DR InParanoid; O25909; -. DR OrthoDB; 9782546at2; -. DR PhylomeDB; O25909; -. DR BRENDA; 2.4.2.19; 2604. DR UniPathway; UPA00253; UER00331. DR EvolutionaryTrace; O25909; -. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central. DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central. DR GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Glycosyltransferase; Pyridine nucleotide biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1..273 FT /note="Probable nicotinate-nucleotide pyrophosphorylase FT [carboxylating]" FT /id="PRO_0000155943" FT BINDING 91 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 124..126 FT /ligand="substrate" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16419067" FT BINDING 158 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16419067" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16419067" FT BINDING 209 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16419067" FT BINDING 235..237 FT /ligand="substrate" FT BINDING 256..258 FT /ligand="substrate" FT HELIX 4..15 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 30..39 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 46..55 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 59..63 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 75..82 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 83..114 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 117..122 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 132..140 FT /evidence="ECO:0007829|PDB:2B7N" FT TURN 141..143 FT /evidence="ECO:0007829|PDB:2B7N" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 159..162 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 168..175 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 185..191 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 192..201 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 204..209 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 213..226 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 231..237 FT /evidence="ECO:0007829|PDB:2B7N" FT TURN 240..242 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 243..247 FT /evidence="ECO:0007829|PDB:2B7N" FT TURN 248..250 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:2B7N" FT HELIX 258..261 FT /evidence="ECO:0007829|PDB:2B7N" FT STRAND 268..271 FT /evidence="ECO:0007829|PDB:2B7N" SQ SEQUENCE 273 AA; 30803 MW; 69CF0F73B2553CD5 CRC64; MEIRTFLERA LKEDLGHGDL FERVLEKDFK ATAFVRAKQE GVFSGEKYAL ELLEMTGIEC VQTIKDKERF KPKDALMEIR GDFSMLLKVE RTLLNLLQHS SGIATLTSRF VEALNSHKVR LLDTRKTRPL LRIFEKYSVL NGGASNHRLG LDDALMLKDT HLRHVKDLKS FLTHARKNLP FTAKIEIECE SFEEAKNAMN AGADIVMCDN LSVLETKEIA AYRDAHYPFV LLEASGNISL ESINAYAKSG VDAISVGALI HQATFIDMHM KMA //