ID   NADC_METTH              Reviewed;         279 AA.
AC   O27860;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=MTH_1832;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB86298.1; -; Genomic_DNA.
DR   PIR; A69112; A69112.
DR   RefSeq; WP_010877434.1; NC_000916.1.
DR   AlphaFoldDB; O27860; -.
DR   SMR; O27860; -.
DR   STRING; 187420.MTH_1832; -.
DR   PRIDE; O27860; -.
DR   EnsemblBacteria; AAB86298; AAB86298; MTH_1832.
DR   GeneID; 1470917; -.
DR   KEGG; mth:MTH_1832; -.
DR   PATRIC; fig|187420.15.peg.1786; -.
DR   HOGENOM; CLU_039622_2_0_2; -.
DR   OMA; DMIMLKD; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000005223; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..279
FT                   /note="Probable nicotinate-nucleotide pyrophosphorylase
FT                   [carboxylating]"
FT                   /id="PRO_0000155953"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         238..240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         259..261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   279 AA;  30806 MW;  0A2B9F69DF026881 CRC64;
     MMDIIREMIR ADVGFEDITT EALIDRGTRV VADIVSREEG VVAGVEVAEM MAREFSISII
     RWKDDGDPLS GGERVLTLEG DAMDILMVER TMLNLMMKMS GIATLTRSML QRARAVNEGI
     RIAATRKTTP GLQWFEKQAV RIGGGDTHRF RLDDCAMIKD NHIAIVGNIE DAVRRVRDHV
     SFTKKVEVEV ESPDDAVRAA EAGADIVLLD NMSPETIRNT LEELERRGLR DNVIVEASGG
     IKPDNIELYA STGVEVISMG FITASAHPVD LSLEIRGLK