ID NPT1_SCHPO Reviewed; 410 AA. AC Q9UTK3; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=Probable nicotinate phosphoribosyltransferase; DE Short=NAPRTase; DE EC=6.3.4.21 {ECO:0000250|UniProtKB:P39683}; GN ORFNames=SPAC1486.06; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). 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 Helps prevent cellular oxidative stress via its role in NAD CC biosynthesis. {ECO:0000250|UniProtKB:Q6XQN6}. 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:0000250|UniProtKB:P39683}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q6XQN6}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:Q6XQN6}; CC Note=Activity is highest with Mn(2+). {ECO:0000250|UniProtKB:Q6XQN6}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D- CC ribonucleotide from nicotinate: step 1/1. CC {ECO:0000250|UniProtKB:Q6XQN6}. 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:0000250|UniProtKB:P22253}. CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU329670; CAB62416.1; -; Genomic_DNA. DR PIR; T50075; T50075. DR RefSeq; NP_594094.1; NM_001019518.2. DR AlphaFoldDB; Q9UTK3; -. DR SMR; Q9UTK3; -. DR STRING; 284812.Q9UTK3; -. DR MaxQB; Q9UTK3; -. DR PaxDb; 4896-SPAC1486-06-1; -. DR EnsemblFungi; SPAC1486.06.1; SPAC1486.06.1:pep; SPAC1486.06. DR PomBase; SPAC1486.06; -. DR VEuPathDB; FungiDB:SPAC1486.06; -. DR eggNOG; KOG2511; Eukaryota. DR HOGENOM; CLU_030991_0_0_1; -. DR InParanoid; Q9UTK3; -. DR OMA; IEHCLEY; -. DR PhylomeDB; Q9UTK3; -. DR UniPathway; UPA00253; UER00457. DR PRO; PR:Q9UTK3; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; HDA:PomBase. DR GO; GO:0005634; C:nucleus; HDA:PomBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 GO; GO:0019358; P:nicotinate nucleotide salvage; ISO:PomBase. DR CDD; cd01401; PncB_like; 1. DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1. DR HAMAP; MF_00570; NAPRTase; 1. DR InterPro; IPR041525; N/Namide_PRibTrfase. DR InterPro; IPR040727; NAPRTase_N. DR InterPro; IPR006406; Nic_PRibTrfase. DR InterPro; IPR007229; Nic_PRibTrfase-Fam. DR InterPro; IPR036068; Nicotinate_pribotase-like_C. DR NCBIfam; TIGR01514; NAPRTase; 1. DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF04095; NAPRTase; 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; Magnesium; Manganese; Metal-binding; Phosphoprotein; KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1..410 FT /note="Probable nicotinate phosphoribosyltransferase" FT /id="PRO_0000205861" FT BINDING 15 FT /ligand="nicotinate" FT /ligand_id="ChEBI:CHEBI:32544" FT /evidence="ECO:0000250|UniProtKB:Q9HJ28" FT BINDING 170 FT /ligand="nicotinate" FT /ligand_id="ChEBI:CHEBI:32544" FT /evidence="ECO:0000250|UniProtKB:Q9HJ28" FT BINDING 220 FT /ligand="nicotinate" FT /ligand_id="ChEBI:CHEBI:32544" FT /evidence="ECO:0000250|UniProtKB:Q9HJ28" FT BINDING 348 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000250|UniProtKB:Q9HJ28" FT MOD_RES 223 FT /note="Phosphohistidine" FT /evidence="ECO:0000250|UniProtKB:P22253" SQ SEQUENCE 410 AA; 46694 MW; E4230ADD9ABA6077 CRC64; MSEPAVVSIL DTDLYKLTML QAVLEHYPDA QVSYKYTNRS PKMALNQEAY NWLREQIRGL RNLHLLPEEE QWLRKNCPYL KESFYEFMHE FEFDPENSIS LNYDSETKDL SIFIHGLWKN TIFYEIPLLA LVSESYFKFV DKDWSPEGQF EKAYEKGKRL IRAGCAFTDF GTRRRRDPHT QEIVLQGLMK AQEDFKGPGS FLGTSNVYFA AKYNLNVSGT VAHEWYMGIA AITQNYKQAN RIASLKWVQT FGTSLLIALT DTFSTDVFLK SFTANSADDL ANVFHGVRQD SGCAEEYIEK VVKHYKSIGV DPSTKVIVHS DALNVDRCIE LYKYCEKCGI KSAFGIGTNL TSDFQKVSNP SEVSKPMNIV IKLFSAEGTK AVKISDDIMK NTGDRDAVIQ AKHQLCLPIA //