ID I2DPQ4_9BURK Unreviewed; 293 AA. AC I2DPQ4; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-OCT-2020, entry version 37. DE RecName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|ARBA:ARBA00019936}; DE EC=2.4.2.19 {ECO:0000256|ARBA:ARBA00011944}; GN ORFNames=MYA_2270 {ECO:0000313|EMBL:AFJ86630.1}; OS Burkholderia sp. KJ006. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ86630.1, ECO:0000313|Proteomes:UP000010108}; RN [1] {ECO:0000313|EMBL:AFJ86630.1, ECO:0000313|Proteomes:UP000010108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KJ006 {ECO:0000313|EMBL:AFJ86630.1, RC ECO:0000313|Proteomes:UP000010108}; RX PubMed=22843575; DOI=10.1128/JB.00821-12; RA Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K., RA Lee C.H., Yu D.S., Park S.H., Kim J.F.; RT "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp. RT Strain KJ006."; RL J. Bacteriol. 194:4432-4433(2012). CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA). CC {ECO:0000256|ARBA:ARBA00003237}. 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 Evidence={ECO:0000256|ARBA:ARBA00000260}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP003514; AFJ86630.1; -; Genomic_DNA. DR RefSeq; WP_014723489.1; NC_017920.1. DR EnsemblBacteria; AFJ86630; AFJ86630; MYA_2270. DR KEGG; buk:MYA_2270; -. DR PATRIC; fig|416344.3.peg.2314; -. DR HOGENOM; CLU_039622_0_3_4; -. DR KO; K00767; -. DR OrthoDB; 1718114at2; -. DR BioCyc; BSP416344:G1H5D-2247-MONOMER; -. DR UniPathway; UPA00253; UER00331. DR Proteomes; UP000010108; Chromosome 1. 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 {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000256|PIRNR:PIRNR006250, ECO:0000313|EMBL:AFJ86630.1}; KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250, KW ECO:0000313|EMBL:AFJ86630.1}. FT DOMAIN 37..124 FT /note="QRPTase_N" FT /evidence="ECO:0000259|Pfam:PF02749" FT DOMAIN 126..290 FT /note="QRPTase_C" FT /evidence="ECO:0000259|Pfam:PF01729" FT REGION 147..149 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1" FT REGION 254..256 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1" FT REGION 275..277 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1" FT BINDING 114 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1" FT BINDING 171 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1" FT BINDING 181 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1" FT BINDING 210 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1" FT BINDING 231 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1" SQ SEQUENCE 293 AA; 31586 MW; 384AA16695A598BB CRC64; MSDAVSPLFD SVRVQYGAAF DEAIARNVAD AIAEDVGACD QTGRLVPADE RRRARIIVRE EAVLCGVPWF EAVIARIDPS IVVQWRYREG DRMTADSTVC ELDGPARALL TAERNGLNFL QLLSGVATAT RRYVDRVEGT RAKILDTRKT LPGLRLAQKY AVRVGGGENQ RLALYDGILI KENHIAAAGG VGEALDAAFA LNAGVPVQIE VETLAQLDTA LAHGAQSVLL DNFTLDMMRE AVRVAAGKAV LEVSGGVNFD TVRTFAETGV DRISIGALTK DVRATDYSMR IVD //