NPT1_YEAST
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 03-AUG-2022, entry version 185.
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;
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 (1.75 ANGSTROMS) 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 + 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: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 PDBsum; 1VLP; -.
DR AlphaFoldDB; P39683; -.
DR SMR; P39683; -.
DR BioGRID; 34604; 204.
DR DIP; DIP-4984N; -.
DR IntAct; P39683; 9.
DR MINT; P39683; -.
DR STRING; 4932.YOR209C; -.
DR iPTMnet; P39683; -.
DR MaxQB; P39683; -.
DR PaxDb; P39683; -.
DR PRIDE; P39683; -.
DR EnsemblFungi; YOR209C_mRNA; YOR209C; YOR209C.
DR GeneID; 854384; -.
DR KEGG; sce:YOR209C; -.
DR SGD; S000005735; NPT1.
DR VEuPathDB; FungiDB:YOR209C; -.
DR eggNOG; KOG2511; Eukaryota.
DR GeneTree; ENSGT00940000153456; -.
DR HOGENOM; CLU_030991_0_0_1; -.
DR InParanoid; P39683; -.
DR OMA; QAVFHRY; -.
DR BioCyc; YEAST:YOR209C-MON; -.
DR BRENDA; 6.3.4.21; 984.
DR UniPathway; UPA00253; UER00457.
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:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
DR GO; GO:0019358; P:nicotinate nucleotide salvage; IDA:SGD.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR CDD; cd01401; PncB_like; 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 PANTHER; PTHR11098; PTHR11098; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR01514; NAPRTase; 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 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..146
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..312
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"
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
