ID A0A133XR21_9BACT Unreviewed; 288 AA.
AC A0A133XR21;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=HMPREF1869_01702 {ECO:0000313|EMBL:KXB33380.1};
OS Bacteroidales bacterium KA00251.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1497953 {ECO:0000313|EMBL:KXB33380.1, ECO:0000313|Proteomes:UP000070662};
RN [1] {ECO:0000313|EMBL:KXB33380.1, ECO:0000313|Proteomes:UP000070662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00251 {ECO:0000313|EMBL:KXB33380.1,
RC ECO:0000313|Proteomes:UP000070662};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXB33380.1}.
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; LSCS01000102; KXB33380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133XR21; -.
DR STRING; 1497953.HMPREF1869_01702; -.
DR PATRIC; fig|1497953.3.peg.1687; -.
DR OrthoDB; 9782546at2; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000070662; 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:UP000070662};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT DOMAIN 27..115
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 117..285
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 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 250..252
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 271..273
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ SEQUENCE 288 AA; 31336 MW; 6085EBD2665AA02D CRC64;
MHTAPHSSIE LNYIDQIIDL ALEEDLGLGD ISTSVLNVPQ ATAQAELTAK EAGFISGIFV
AQLVASKVDP EVQFEALVTD GSPISKGDLL IRLKGNATSL LGMERTMLNF LQRMSGIATT
TAQYVQAVGP HKTVIVDTRK TAPGMRYIDK MAVRHGGGTN HRIDLSSMVM LKDNHVRLIQ
ESGKSFEQII EQARRSLPLS TRIEVETTNL KEVERALKAG VDVIMLDNMT LEEMKQAVSL
INGECMVEAS GNMTLDRIPQ VAAIGVDYIS VGALTHSIKA FDISMNFI
//