ID A5I1P2_CLOBH Unreviewed; 493 AA.
AC A5I1P2; A7G3E7;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 112.
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 OrderedLocusNames=CBO1410 {ECO:0000313|EMBL:CAL82954.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82954.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL82954.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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; AM412317; CAL82954.1; -; Genomic_DNA.
DR RefSeq; WP_011949007.1; NC_009698.1.
DR RefSeq; YP_001253927.1; NC_009495.1.
DR RefSeq; YP_001387312.1; NC_009698.1.
DR AlphaFoldDB; A5I1P2; -.
DR GeneID; 5185665; -.
DR KEGG; cbh:CLC_1447; -.
DR KEGG; cbo:CBO1410; -.
DR PATRIC; fig|413999.7.peg.1390; -.
DR HOGENOM; CLU_025154_2_1_9; -.
DR OMA; TDTFAIQ; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
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; 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; 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 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:UP000001986};
KW Transferase {ECO:0000256|RuleBase:RU365100}.
FT DOMAIN 17..141
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 371..480
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 493 AA; 56377 MW; EA975AF2871ABAEA CRC64;
MEYSKNFDVR NNRNLTMLVD FYELTMGNGY LKSGMGDKIA YYDMFFRRVP DGGGYCIMAG
VQQLIEYLSG LKFTEDDIEY LRSKKEFSEE FLDYLKNFKF SCDVWAVPEG YPVFPNEPLV
TVRGPAIQAQ FVETMILLTI NHQTLIATKA NRICRAAENR SVMEFGSRRA QGYDGAIYGA
RAAVIGGCNA TACTIAEEMF GIPAAGTMAH SWIQLFPTEY EAFKAWAEVN PENCVLLVDT
YNVLKSGIPN AIKVFNEVLR PKGIRPKGIR IDSGDITYLT KICRKMLDDA GYKDVGIVVS
NSLDEFIIRD VLNQGAKIDS FGVGERLITA KSEPVFGGVY KLVAVEAYDG IITPKIKISE
NEEKITNPGF KKLYRIYDKN SHQAIADLIT MHDEKIDESK PLEIFNPLFT WKKKKIKDYY
VEELLVKIFN KGKQVYESPD VMDIKAFAKK QTERFWPEVL RFENPHKYYV DLSPKLWRVK
QELLHKFSDT YEE
//