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Database: UniProt
Entry: A0A0J1DP00_9FIRM
LinkDB: A0A0J1DP00_9FIRM
Original site: A0A0J1DP00_9FIRM 
ID   A0A0J1DP00_9FIRM        Unreviewed;       344 AA.
AC   A0A0J1DP00;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN   ORFNames=AA931_03875 {ECO:0000313|EMBL:KLU40695.1};
OS   Peptococcaceae bacterium 1109.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1655638 {ECO:0000313|EMBL:KLU40695.1, ECO:0000313|Proteomes:UP000036486};
RN   [1] {ECO:0000313|EMBL:KLU40695.1, ECO:0000313|Proteomes:UP000036486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1109 {ECO:0000313|EMBL:KLU40695.1};
RA   Town J.R., Dumonceaux T.J.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC         nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide +
CC         phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:456216; EC=6.3.4.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001240};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004952}.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family.
CC       {ECO:0000256|ARBA:ARBA00009400}.
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:KLU40695.1}.
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DR   EMBL; LDJB01000001; KLU40695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1DP00; -.
DR   STRING; 1655638.AA931_03875; -.
DR   PATRIC; fig|1655638.3.peg.783; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000036486; Unassembled WGS sequence.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01571; NAPRTase_B; 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; IPR035809; NAPRTase_arc-type.
DR   InterPro; IPR007229; Nic_PRibTrfase-Fam.
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; PTHR43202:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43202; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE; 1.
DR   Pfam; PF01729; QRPTase_C; 1.
DR   Pfam; PF02749; QRPTase_N; 1.
DR   PIRSF; PIRSF000484; NAPRT; 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:0000313|EMBL:KLU40695.1}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KLU40695.1}.
FT   DOMAIN          48..124
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          128..316
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   344 AA;  36608 MW;  BFBCCC41FAD5B5AC CRC64;
     MKFIKTVQEV ADFTVSGDRK LFSATHEEVE AGLTTDIYFV KTREILEKLG RADTVVAAEI
     FARGAGVFAG VEEVKRLLAE TGVEVWSLPE GEKFAPKEVV MRIFGPYGQF GIYETAVLGI
     LASSSAWATR AREAKEAAGG KPAICFGARH VHPAVAPVME RAAVIGGADG ASCILGAKIA
     GIEPMGTVPH ALFLIVGDTV EAALGYDEHM PPSSPRSMLV DTFKDEVEES LRLCEAMGTR
     LESVRLDTPG ERGGVTPGLV AELRAKLDLA GYSHVRIFVS GGLDPDRIRL LSEAGADAFG
     VGSYISGASP IDMTMDLKEV DGKPVAKRGR IPGLTPSKRL VRIL
//
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