ID T5D193_HELPX Unreviewed; 273 AA.
AC T5D193;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=N406_02560 {ECO:0000313|EMBL:EQL64137.1};
OS Helicobacter pylori FD577.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1191283 {ECO:0000313|EMBL:EQL64137.1, ECO:0000313|Proteomes:UP000015967};
RN [1] {ECO:0000313|EMBL:EQL64137.1, ECO:0000313|Proteomes:UP000015967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD577 {ECO:0000313|EMBL:EQL64137.1,
RC ECO:0000313|Proteomes:UP000015967};
RX PubMed=23012278; DOI=10.1128/JB.01278-12;
RA Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT cultured from patients with functional dyspepsia and gastric cancer.";
RL J. Bacteriol. 194:5695-5696(2012).
RN [2] {ECO:0000313|EMBL:EQL64137.1, ECO:0000313|Proteomes:UP000015967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD577 {ECO:0000313|EMBL:EQL64137.1,
RC ECO:0000313|Proteomes:UP000015967};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(2013).
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:EQL64137.1}.
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DR EMBL; AKHR02000005; EQL64137.1; -; Genomic_DNA.
DR RefSeq; WP_000404081.1; NZ_AKHR02000005.1.
DR AlphaFoldDB; T5D193; -.
DR PATRIC; fig|1191283.4.peg.1586; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000015967; 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 16..101
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 103..271
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 124..126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 235..237
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 256..258
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ SEQUENCE 273 AA; 30753 MW; 7534BF71CC84FFB2 CRC64;
MEIKTFLEGA LKEDLGHGDL FERVLEKDFK ATAFVRAKQE GVFSGERYAL ELLEMTGIEC
VKTINDKERF KPKDTLMEIR GDFSMLLKVE RTLLNLLQHS SGIATLTSRF VEALNSHEVR
LLDTRKTRPL LRIFEKYSVL NGGASNHRLG LDDALMLKDT HLKHVKDLKS FLTHARKNLP
FTAKIEIECE SFEEAKNAMN AGADIVMCDN LSVLETKEIA AYRDMHYPFV LLEASGNISL
ESINAYAKSG VDAISVGALI HQATFIDMHM KMA
//
