NADC_HELPY
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 03-AUG-2022, entry version 125.
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; Proteobacteria; 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}.
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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.C694_06995; -.
DR PaxDb; O25909; -.
DR EnsemblBacteria; AAD08397; AAD08397; HP_1355.
DR KEGG; hpy:HP_1355; -.
DR PATRIC; fig|85962.47.peg.1451; -.
DR eggNOG; COG0157; Bacteria.
DR OMA; DMIMLKD; -.
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; -; 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 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
