ID   NPT1_YEAST              Reviewed;         429 AA.
AC   P39683; D6W2R5; Q08626;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   04-NOV-2026, entry version 202.
DE   RecName: Full=Nicotinate phosphoribosyltransferase;
DE            Short=NAPRTase;
DE            EC=6.3.4.21 {ECO:0000269|PubMed:9521740};
GN   Name=NPT1; OrderedLocusNames=YOR209C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RA   Lalo D., Doira C., Thuriaux P.;
RT   "The BRF1-STE4 region chromosome XV contains eleven genes: two of them
RT   define distinct RNA polymerase subunits and one encodes a putative
RT   nicotinate phosphoribosyl transferase.";
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874; DOI=10.1038/387s098;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
RC   STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX   PubMed=8516295; DOI=10.1073/pnas.90.12.5524;
RA   Lalo D., Carles C., Sentenac A., Thuriaux P.;
RT   "Interactions between three common subunits of yeast RNA polymerases I and
RT   III.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5524-5528(1993).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND PHOSPHORYLATION.
RX   PubMed=9521740; DOI=10.1021/bi9720134;
RA   Rajavel M., Lalo D., Gross J.W., Grubmeyer C.;
RT   "Conversion of a cosubstrate to an inhibitor: phosphorylation mutants of
RT   nicotinic acid phosphoribosyltransferase.";
RL   Biochemistry 37:4181-4188(1998).
RN   [6]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=12062417; DOI=10.1016/s0014-5793(02)02585-1;
RA   Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M.,
RA   Rytka J., Herbert C.J.;
RT   "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae.";
RL   FEBS Lett. 517:97-102(2002).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9] {ECO:0007744|PDB:1VLP}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH PHOSPHATE.
RX   PubMed=16154095; DOI=10.1016/j.str.2005.05.016;
RA   Chappie J.S., Canaves J.M., Han G.W., Rife C.L., Xu Q., Stevens R.C.;
RT   "The structure of a eukaryotic nicotinic acid phosphoribosyltransferase
RT   reveals structural heterogeneity among type II PRTases.";
RL   Structure 13:1385-1396(2005).
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       (PubMed:9521740). Essential for growth under anaerobic conditions
CC       (PubMed:12062417). {ECO:0000269|PubMed:12062417,
CC       ECO:0000269|PubMed:9521740}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-alpha-D-ribose 1-diphosphate + nicotinate + ATP +
CC         H2O = nicotinate beta-D-ribonucleotide + ADP + phosphate +
CC         diphosphate; 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:0000269|PubMed:9521740};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1. {ECO:0000269|PubMed:9521740,
CC       ECO:0000305|PubMed:12062417}.
CC   -!- INTERACTION:
CC       P39683; P33203: PRP40; NbExp=2; IntAct=EBI-12218, EBI-701;
CC       P39683; P39940: RSP5; NbExp=2; IntAct=EBI-12218, EBI-16219;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC       cycle (By similarity). Phosphorylation strongly increases the affinity
CC       for substrates and increases the rate of nicotinate D-ribonucleotide
CC       production (PubMed:9521740). Dephosphorylation regenerates the low-
CC       affinity form of the enzyme, leading to product release (By
CC       similarity). {ECO:0000250|UniProtKB:P22253,
CC       ECO:0000269|PubMed:9521740}.
CC   -!- MISCELLANEOUS: Present with 32100 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
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DR   EMBL; Z36878; CAA85352.1; -; Genomic_DNA.
DR   EMBL; Z75117; CAA99424.1; -; Genomic_DNA.
DR   EMBL; L11274; AAB59317.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10981.1; -; Genomic_DNA.
DR   PIR; S67101; S67101.
DR   RefSeq; NP_014852.1; NM_001183628.1.
DR   PDB; 1VLP; X-ray; 1.75 A; A/B/C/D=1-429.
DR   AlphaFoldDB; P39683; -.
DR   SMR; P39683; -.
DR   BioGRID; 34604; 213.
DR   DIP; DIP-4984N; -.
DR   FunCoup; P39683; 272.
DR   IntAct; P39683; 9.
DR   STRING; 4932.YOR209C; -.
DR   iPTMnet; P39683; -.
DR   PaxDb; 4932-YOR209C; -.
DR   PeptideAtlas; P39683; -.
DR   EnsemblFungi; YOR209C_mRNA; YOR209C; YOR209C.
DR   GeneID; 854384; -.
DR   KEGG; sce:YOR209C; -.
DR   AGR; SGD:S000005735; -.
DR   SGD; S000005735; NPT1.
DR   VEuPathDB; FungiDB:YOR209C; -.
DR   eggNOG; KOG2511; Eukaryota.
DR   HOGENOM; CLU_030991_0_0_1; -.
DR   InParanoid; P39683; -.
DR   OMA; AAFEFHC; -.
DR   OrthoDB; 193380at2759; -.
DR   BioCyc; YEAST:YOR209C-MONOMER; -.
DR   BRENDA; 6.3.4.21; 984.
DR   UniPathway; UPA00253; UER00457.
DR   BioGRID-ORCS; 854384; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P39683; -.
DR   PRO; PR:P39683; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P39683; protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IDA:SGD.
DR   GO; GO:0034355; P:NAD+ biosynthetic process via the salvage pathway; IBA:GO_Central.
DR   GO; GO:0019358; P:nicotinate nucleotide salvage; IDA:SGD.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IMP:SGD.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD.
DR   CDD; cd01401; PncB_like; 1.
DR   FunFam; 3.20.140.10:FF:000009; Nicotinate phosphoribosyltransferase; 1.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Ligase; Nucleus; Phosphoprotein;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..429
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_0000205862"
FT   BINDING         15
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         177
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         229
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         294
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         355
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000305|PubMed:16154095"
FT   MOD_RES         232
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P22253"
FT   CONFLICT        131..137
FT                   /note="YEIPLLS -> MRSLTV (in Ref. 1; CAA85352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144..158
FT                   /note="FKFVDIDWDYENQLE -> LIVTSTGLRNHR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175..177
FT                   /note="SEF -> RIH (in Ref. 1; CAA85352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="E -> EL (in Ref. 1; CAA85352)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1..4
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           14..26
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          31..39
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           47..59
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           67..76
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           97..100
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          101..108
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          111..124
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           125..128
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           132..142
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           143..147
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           156..169
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           185..201
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           203..206
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   TURN            207..209
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          210..215
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           216..222
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           232..242
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           248..260
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           262..264
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          267..269
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           275..279
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           286..289
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          292..295
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           300..308
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           309..314
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          321..326
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           332..344
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          348..353
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           355..358
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          369..371
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   STRAND          376..383
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   HELIX           402..411
FT                   /evidence="ECO:0007829|PDB:1VLP"
FT   TURN            416..418
FT                   /evidence="ECO:0007829|PDB:1VLP"
SQ   SEQUENCE   429 AA;  49019 MW;  F3F7941476C3398B CRC64;
     MSEPVIKSLL DTDMYKITMH AAVFTNFPDV TVTYKYTNRS SQLTFNKEAI NWLKEQFSYL
     GNLRFTEEEI EYLKQEIPYL PSAYIKYISS SNYKLHPEEQ ISFTSEEIEG KPTHYKLKIL
     VSGSWKDTIL YEIPLLSLIS EAYFKFVDID WDYENQLEQA EKKAETLFDN GIRFSEFGTR
     RRRSLKAQDL IMQGIMKAVN GNPDRNKSLL LGTSNILFAK KYGVKPIGTV AHEWVMGVAS
     ISEDYLHANK NAMDCWINTF GAKNAGLALT DTFGTDDFLK SFRPPYSDAY VGVRQDSGDP
     VEYTKKISHH YHDVLKLPKF SKIICYSDSL NVEKAITYSH AAKENGMLAT FGIGTNFTND
     FRKKSEPQVK SEPLNIVIKL LEVNGNHAIK ISDNLGKNMG DPATVKRVKE ELGYTERSWS
     GDNEAHRWT
//