ID   NADC_MYCLE              Reviewed;         284 AA.
AC   P46714;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE            EC=2.4.2.19;
DE   AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE            Short=QAPRTase;
GN   Name=nadC; OrderedLocusNames=ML1227; ORFNames=B1170_C1_168;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC31608.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U00010; AAA17060.1; -; Genomic_DNA.
DR   EMBL; AL583921; CAC31608.1; ALT_INIT; Genomic_DNA.
DR   PIR; E87062; E87062.
DR   PIR; S72696; S72696.
DR   AlphaFoldDB; P46714; -.
DR   SMR; P46714; -.
DR   STRING; 272631.ML1227; -.
DR   EnsemblBacteria; CAC31608; CAC31608; CAC31608.
DR   KEGG; mle:ML1227; -.
DR   Leproma; ML1227; -.
DR   eggNOG; COG0157; Bacteria.
DR   HOGENOM; CLU_039622_0_0_11; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000000806; 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..284
FT                   /note="Nicotinate-nucleotide pyrophosphorylase
FT                   [carboxylating]"
FT                   /id="PRO_0000155945"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247..249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         268..270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  30308 MW;  D2EE754D8759933B CRC64;
     MLSDCEFDAA RDTIRRALHE DLRYGLDITT QATVPAGTVV TGSMVPREPG VIAGVDVALL
     VLDEVFGVDG YRVLYRVEDG ARLQSGQPLL TVQAAARGLL TAERTMLNLV CHMSGIATVT
     VAWVDAVRGT KAKIRDTRKT LPGLRALQKY AVRVGGGVNH RLGLGDTALI KDNHVAAVGS
     VVDALRAVRA AAPELPCEVE VDSLEQLDAM LAEEPELILL DNFPVWQTQV AVQRRDIRAP
     TVLLESSGGL SLENAAIYAG TGVDYLAVGA LTHSVRILDI GLDL