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Database: UniProt
Entry: A0A410UGM6_9GAMM
LinkDB: A0A410UGM6_9GAMM
Original site: A0A410UGM6_9GAMM 
ID   A0A410UGM6_9GAMM        Unreviewed;       285 AA.
AC   A0A410UGM6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   Name=nadC {ECO:0000313|EMBL:QAU23373.1};
GN   ORFNames=EO087_04740 {ECO:0000313|EMBL:QAU23373.1};
OS   Dyella sp. M7H15-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=2501295 {ECO:0000313|EMBL:QAU23373.1, ECO:0000313|Proteomes:UP000288967};
RN   [1] {ECO:0000313|EMBL:QAU23373.1, ECO:0000313|Proteomes:UP000288967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M7H15-1 {ECO:0000313|EMBL:QAU23373.1,
RC   ECO:0000313|Proteomes:UP000288967};
RA   Gao Z.-H., Qiu L.-H., Yang Z.;
RT   "Dyella phosphatilytica sp. nov. strain M7H15-1T., a phosphate solubilizing
RT   bacterium isolated from forest soil and analysis of the complete genome
RT   sequence.";
RL   Submitted (JAN-2019) 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; CP035300; QAU23373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A410UGM6; -.
DR   KEGG; dye:EO087_04740; -.
DR   OrthoDB; 9782546at2; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000288967; 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; 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:UP000288967};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          28..115
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          118..281
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         138..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         245..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         266..268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ   SEQUENCE   285 AA;  30365 MW;  F5020892AC6C3215 CRC64;
     MSTALRFTPP DQAVIHADVE RAFAEDLGKG DATASLLSAD AKATAQLICR EDAVIAGIPW
     FNAAVRKLDP EARIDWNVSD GDRATPGTVI CEVHGNARAL LSAERTSLNF LQLLSGTATH
     TAAHVAAVAG TKVCVLDTRK TIPGLRLAQK YAVLCGGGHN HRIGLYDAIL VKENHIIAAG
     SIAAAVKAAR KLHPSLLLEV EVENLNELQQ ALDAGVDRIM LDNFTLPLIR EAVTQTAGRV
     PLEISGNVDL NTIGDYARTG VDYISVGALT KHVRAIDLSL RLKVH
//
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