ID A0A0D1A7T5_9LACO Unreviewed; 488 AA.
AC A0A0D1A7T5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=pncB {ECO:0000313|EMBL:KIS03772.1};
GN ORFNames=WDC_0603 {ECO:0000313|EMBL:KIS03772.1};
OS Paucilactobacillus wasatchensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1335616 {ECO:0000313|EMBL:KIS03772.1, ECO:0000313|Proteomes:UP000032279};
RN [1] {ECO:0000313|EMBL:KIS03772.1, ECO:0000313|Proteomes:UP000032279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDC04 {ECO:0000313|EMBL:KIS03772.1,
RC ECO:0000313|Proteomes:UP000032279};
RA Oberg C.J., Culumber M., McMahon D.J., Broadbent J.R., Oberg T.S.,
RA Ortaki F.;
RT "Lactobacillus wasatchii sp. WDC04, a late gas producing bacteria isolated
RT from aged chedder cheese.";
RL Submitted (AUG-2013) 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}.
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:KIS03772.1}.
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DR EMBL; AWTT01000010; KIS03772.1; -; Genomic_DNA.
DR RefSeq; WP_044010311.1; NZ_AWTT01000010.1.
DR AlphaFoldDB; A0A0D1A7T5; -.
DR STRING; 1335616.WDC_0603; -.
DR PATRIC; fig|1335616.4.peg.600; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000032279; Unassembled WGS sequence.
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:KIS03772.1};
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:UP000032279};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:KIS03772.1}.
FT DOMAIN 12..136
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 158..335
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 362..471
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 488 AA; 55638 MW; D65C329877078F43 CRC64;
MSYRFPDDSI ALHTDAYELS MMQTYWQKGM AQRRSVFELY FRNMPFGNGY AVFAGLQRVV
SYIQQLKFSD SDIDYLKQTG QFDADFLEYL RDFKFTGSIN STVEGDLVFN NEPILQVDAP
LIGAQLVETA LLNIINYQTL IATKAARIKS VVGDDPLLEF GTRRAQEMDA AIWGTRAAYI
GGFDATSNVR AGKLFGIPIS GTHAHALVQT YMNDYDAFKA YAETHKDCVF LVDTFDTLKS
GVPNAIRVAK EMGDKINFQG VRIDSGDIAY ISKRVREMLD EAGFKDAKVY ASNDLDEKTI
MNLKMQKAKI DVWGVGTKLI TAFDQPALGA VYKLVSFEDE HGQMIDSIKI SSNVTKVSTP
GKKQVWRITD QSDGKTEGDY VTLWDEKPQD KESLYMFNPD YTYINKTLHN FAARPILQPI
FTNGKLVYDL PELDEIKLFS KRHLDMLWDE YKRDLNPQVY PVDLSQECFD NKMKIIKQVR
DYVNQLKF
//
