ID A0A385NQB6_9BACI Unreviewed; 489 AA.
AC A0A385NQB6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DOE78_14560 {ECO:0000313|EMBL:AYA76561.1};
OS Bacillus sp. Y1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=352858 {ECO:0000313|EMBL:AYA76561.1, ECO:0000313|Proteomes:UP000265711};
RN [1] {ECO:0000313|EMBL:AYA76561.1, ECO:0000313|Proteomes:UP000265711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y1 {ECO:0000313|EMBL:AYA76561.1};
RA Rathod J., Jean J.-S.;
RT "Arsenic resistant and redox active subsurface bacterial isolate Bacillus
RT sp. Y1 from Yichu borehole sediment.";
RL Submitted (JUN-2018) 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; CP030028; AYA76561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A385NQB6; -.
DR KEGG; bacq:DOE78_14560; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000265711; 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:AYA76561.1};
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:UP000265711};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:AYA76561.1}.
FT DOMAIN 12..136
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 158..338
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 363..471
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 489 AA; 55641 MW; 0D61C49423C118DA CRC64;
MKRDYPDDSL TLHTDLYQIN MAETYWEDGI HNKKAVFDLY FRNLPFGNGY AIFAGLERVI
DYIRGFRFTD SDIEYLREVA HYKEDFLDYL KTLTFTGNIR SMVEGEIAFG NEPLLRVEAP
LAEAQLIETA LLNIINYQTL IATKASRIKQ VIGDGVGMEF GTRRAQEMDA AIWGTRAAFI
GGFQATSNVR AGKMFGIPVA GTHAHSLVQA YKDEYIAFHK YARRHKDCVF LVDTYDTLRS
GVPNAIKVAK ELGDKINFLG IRLDSGDLAY LSKKAREMLD EAGFTETKII ASNDLDEYTI
INLKAQGAMI DTWGVGTKLI TAYDQAALGA VYKLVAIEGE NGELVDTIKI SGNPEKVSTP
GLKRVYRIIN NENHKSEGDY ITMDEEHPEA ESRIKMFHPI HTYISKFITN FTAKDLHEDI
FINGKLVYEV PSLLQMQNYV KENLQLLWEE YTRALNPEEY PVDLSQKCWD NKIRNIEEVK
ANIKSQNIR
//
