ID F4BKR6_CARS1 Unreviewed; 472 AA.
AC F4BKR6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 Name=yueK {ECO:0000313|EMBL:AEB29068.1};
GN OrderedLocusNames=CAR_c03470 {ECO:0000313|EMBL:AEB29068.1};
OS Carnobacterium sp. (strain 17-4).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=208596 {ECO:0000313|EMBL:AEB29068.1, ECO:0000313|Proteomes:UP000008304};
RN [1] {ECO:0000313|EMBL:AEB29068.1, ECO:0000313|Proteomes:UP000008304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-4 {ECO:0000313|EMBL:AEB29068.1,
RC ECO:0000313|Proteomes:UP000008304};
RX PubMed=21551290; DOI=10.1128/JB.05113-11;
RA Voget S., Klippel B., Daniel R., Antranikian G.;
RT "Complete gnome sequence of Carnobacterium sp. 17-4.";
RL J. Bacteriol. 193:3403-3404(2011).
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; CP002563; AEB29068.1; -; Genomic_DNA.
DR AlphaFoldDB; F4BKR6; -.
DR STRING; 208596.CAR_c03470; -.
DR KEGG; crn:CAR_c03470; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_025154_2_1_9; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000008304; 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 CDD; cd01570; NAPRTase_A; 1.
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; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR041619; NAPRTase_C.
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:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17956; NAPRTase_C; 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:AEB29068.1};
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:UP000008304};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:AEB29068.1}.
FT DOMAIN 1..116
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 138..317
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 342..451
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 472 AA; 53280 MW; ADB7A8A805FDA76A CRC64;
MMKTYWELGK ADSHAVFESY FRSNPFNSGY AIFAGLERIV QYIQKLKFTS SDIDYLRSLN
TYPEGFLDYL KDFKFKGTIR SMVEGEVVFA GEPLIQVEGP LADCQLVETA ILNVLNYQTL
IATKASNIKS IVKDEPVLEF GTRRAQEMDA AIWGTRAAFI GGCDATSNTR AGKIFDIPVS
GTHAHSLVQV YRNDYDAFIA YATTHKDCVF LVDTYDTLKS GVPNAIRVAR ELGDKINFLG
VRIDSGDMAY ISKKVRQQLD DAGFTEAKIY ASNDLDEKTI LNLKMQGARI DVWGVGTKLI
TAYDQPALGA VYKLVSIEDE QGNMVDTLKL SSNAEKVSTP GKKQVWRITK NDDGKSEGDY
ITLWEERPDQ KEELFMFHPV HTYINKTVTN FSARPLLKEI FVDGKLVYDL PKLTEIKTYA
EVSLGMLWEE YKRSLNPEAY PVDLSQSAYH HKIKSIEKAR DDVNKMSKKP II
//
