ID   NADC_SYNY3              Reviewed;         295 AA.
AC   P74301;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=slr0936;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA18395.1; -; Genomic_DNA.
DR   PIR; S76136; S76136.
DR   AlphaFoldDB; P74301; -.
DR   SMR; P74301; -.
DR   IntAct; P74301; 1.
DR   STRING; 1148.1653482; -.
DR   PaxDb; P74301; -.
DR   EnsemblBacteria; BAA18395; BAA18395; BAA18395.
DR   KEGG; syn:slr0936; -.
DR   eggNOG; COG0157; Bacteria.
DR   InParanoid; P74301; -.
DR   OMA; DMIMLKD; -.
DR   PhylomeDB; P74301; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000001425; 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   3: Inferred from homology;
KW   Glycosyltransferase; Pyridine nucleotide biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..295
FT                   /note="Probable nicotinate-nucleotide pyrophosphorylase
FT                   [carboxylating]"
FT                   /id="PRO_0000155950"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         144..146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         255..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   295 AA;  31973 MW;  DBCF6F88362E0735 CRC64;
     MMRILVTNPA PMTCLPPWII IDPWLQQWLA EDIGRGDWST QGLGLQHRGQ ARWVAKENGV
     IAGLPMAARI FQLLDPSMEF QVLAGEGQAV TASTVVATMA GNLGSLLTGE RVALNLVMGL
     SGIATMTRQY VQAIADYPTR FVDTRKTTPG LRVLEKYASR LGGAMNHRLG LDDAVMVKDN
     HIQAAGSITK AVQTLRQNLP YPLAIEVETS NLEEVQEAIA TQVEIIMLDN MGTDTMATAV
     KLIRQANPLI RIEASGNVTL ANLTAIASTG VDFISSSAPI TRSPWLDLSM QIVRN