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Database: UniProt
Entry: D7JDX1_9BACT
LinkDB: D7JDX1_9BACT
Original site: D7JDX1_9BACT 
ID   D7JDX1_9BACT            Unreviewed;       277 AA.
AC   D7JDX1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=HMPREF0156_00947 {ECO:0000313|EMBL:EFI17352.1};
OS   Bacteroidetes oral taxon 274 str. F0058.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=575590 {ECO:0000313|EMBL:EFI17352.1, ECO:0000313|Proteomes:UP000004685};
RN   [1] {ECO:0000313|Proteomes:UP000004685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0058 {ECO:0000313|Proteomes:UP000004685};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroidetes bacterium Oral taxon 274 strain
RT   F0058.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; GG774889; EFI17352.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7JDX1; -.
DR   STRING; 575590.HMPREF0156_00947; -.
DR   eggNOG; COG0157; Bacteria.
DR   HOGENOM; CLU_039622_0_1_10; -.
DR   OrthoDB; 9782546at2; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000004685; 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   Reference proteome {ECO:0000313|Proteomes:UP000004685};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          14..103
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          105..274
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         126..128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         238..240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         259..261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ   SEQUENCE   277 AA;  31008 MW;  7EE58D11D96AF4E4 CRC64;
     MLEQDIKLWL AEDIGDGDHT TLCCIPADAI GRSRLIVKDT GIIAGIEVAK KVFEIFDNEL
     RIMQYMHDGD EVKPQDIAFE VEGKVRSLLQ TERLMLNIVQ RMSGIATRTR EYVKLLEGTR
     TRILDTRKTT PGLRMLEKDA VLIGGGCNHR IGLYDMILLK DNHIDFAGGI SQAIDRANKY
     LKDNNKNLKI EIEVRNFDEL NEVLASGNVN RIMLDNFSVA DTRKAVEIIG GRFETESSGG
     ITETTIREYA LAGVDYISVG ALTHSIKSLD MSFKAMK
//
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