ID   PNCB_DICDI              Reviewed;         589 AA.
AC   Q55G10; Q6XQM3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Nicotinate phosphoribosyltransferase;
DE            Short=NAPRTase;
DE            EC=6.3.4.21 {ECO:0000250|UniProtKB:Q6XQN6};
GN   Name=naprt; ORFNames=DDB_G0268472;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX4;
RA   Huang C.-H., Peng J., Chen Y.;
RT   "Sequence analysis and molecular evolution of the eukaryotic nicotinate
RT   phosphoribosyltransferase family.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(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       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:Q6XQN6};
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}.
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DR   EMBL; AY214338; AAP69616.1; -; mRNA.
DR   EMBL; AAFI02000003; EAL73689.1; -; Genomic_DNA.
DR   RefSeq; XP_647373.1; XM_642281.1.
DR   AlphaFoldDB; Q55G10; -.
DR   SMR; Q55G10; -.
DR   STRING; 44689.Q55G10; -.
DR   PaxDb; 44689-DDB0215395; -.
DR   EnsemblProtists; EAL73689; EAL73689; DDB_G0268472.
DR   GeneID; 8616182; -.
DR   KEGG; ddi:DDB_G0268472; -.
DR   dictyBase; DDB_G0268472; naprt.
DR   eggNOG; KOG2511; Eukaryota.
DR   HOGENOM; CLU_025154_1_0_1; -.
DR   InParanoid; Q55G10; -.
DR   OMA; NPHIYKV; -.
DR   PhylomeDB; Q55G10; -.
DR   Reactome; R-DDI-197264; Nicotinamide salvaging.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   UniPathway; UPA00253; UER00457.
DR   PRO; PR:Q55G10; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   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   2: Evidence at transcript level;
KW   Ligase; Magnesium; Manganese; Metal-binding; Phosphoprotein;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..589
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_0000371328"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         256
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         356
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         418
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   MOD_RES         259
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P22253"
FT   CONFLICT        487
FT                   /note="S -> F (in Ref. 1; AAP69616)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   589 AA;  66085 MW;  D74F67EFBDE070C2 CRC64;
     MSQSNTPLKR KKTENGYSEN GSTTGATSNQ IRELKRATTV DYVYRDQESK DKIKPLNGFV
     TPLLTDLYQI TMAYSLWKNN RHEIPAVFDL YFRKSPFGGE FTVFAGLEEV IRFVSDFHYT
     KEEVGFIKEM IPDCEQEFLD YLSKLDSSSV TLYAMKEGSV VFPRVPLLRV EGPMILCQLF
     ETTLLCLVNF ASLVATNAAR HRLAVGKEKV MLEFGLRRAQ GPDGAMSASR YSYLGGADGT
     SNVLAHCFFG IPIRGTHAHS FITNYSGPDE LLDASIKDTN GNVHNLLEMS QKYRDELGYT
     ATNLSELVAF VAYARTFPNG LVALVDTYDT LASGVPNFIC VALALHQLGY KAVGIRLDSG
     DLSYLSKASR KLFKQIGEQF KIDYFEKFSI VASNDLNEPT IIALNRQGHE IDVFAIGTNL
     VTCQAQPALG CVYKLVEING SPRIKLSQEA NKITLPGRKT AYRLFGSEGH PLVDLLVDDN
     DMIKDGSKQI PQVGKKVLCL HPFEEQKRVI VTPVQIEKLH HIVFEKGQLT MPLPALNDIR
     EYCFQQISKV REDHLRNSNP TPYKVSVTKE LFDTLHNLWL DSVPIKEMK
//