ID A0A1Q2CNG8_9ACTN Unreviewed; 450 AA.
AC A0A1Q2CNG8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN ORFNames=BW730_09290 {ECO:0000313|EMBL:AQP47657.1};
OS Tessaracoccus aquimaris.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1332264 {ECO:0000313|EMBL:AQP47657.1, ECO:0000313|Proteomes:UP000188145};
RN [1] {ECO:0000313|Proteomes:UP000188145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSG39 {ECO:0000313|Proteomes:UP000188145};
RA Tak E.J., Bae J.-W.;
RT "Tessaracoccus aquaemaris sp. nov., isolated from the intestine of a Korean
RT rockfish, Sebastes schlegelii, in a marine aquaculture pond.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC {ECO:0000256|RuleBase:RU365100}.
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 ECO:0000256|RuleBase:RU365100};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
CC -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC cycle. Phosphorylation strongly increases the affinity for substrates
CC and increases the rate of nicotinate D-ribonucleotide production.
CC Dephosphorylation regenerates the low-affinity form of the enzyme,
CC leading to product release. {ECO:0000256|RuleBase:RU365100}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
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DR EMBL; CP019606; AQP47657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2CNG8; -.
DR STRING; 1332264.BW730_09290; -.
DR KEGG; tes:BW730_09290; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000188145; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR NCBIfam; TIGR01513; NAPRTase_put; 1.
DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11098:SF8; NICOTINATE PHOSPHORIBOSYLTRANSFERASE PNCB1; 1.
DR Pfam; PF17767; NAPRTase_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:0000313|EMBL:AQP47657.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365100};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU365100};
KW Reference proteome {ECO:0000313|Proteomes:UP000188145};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:AQP47657.1}.
FT DOMAIN 5..128
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
SQ SEQUENCE 450 AA; 48655 MW; D8B1F90ECE94E1F5 CRC64;
MTTALLTDHY ELTMVQAAMD AGTANRRSLF DLFTRRLPEG RRYGVAAGLG RAIDAIENFR
FGEEELSFLI ERRVIRENLA EWLANYRFNG DIWGYAEGEV YFPGSPVLSV EGTFAEACIL
ETVLLSIYNH DSAIAAAGSR MTAMAGERRC AEMGSRRTHE WAAAAAARAA YIAGFASTSN
LEAGRSFGVP TIGTAAHSFT LLHDTEEDAF RAQLGSLGED TTLLVDTYDV EAAIRKGVEL
TEGRLGSIRL DSGDLAIMAR QARDLLDDLG ATETKIMVTS DLDEWQIALL QGAPVDGYGV
GTSLVTGSGH PTCGFVYKLV ARAASDAPDA EWVSVGKKSK GKNTLGGRKF AMRRRGEDGR
AETEVIGLGA PPVNDGNDRD LLVPIFQDGR RVYEATLDDA RRRHAESLAE LPLAARRISK
GDPALETLIL DEAGDETTNP YQAAPIVTNL
//
