PNCB_DICDI
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 03-AUG-2022, entry version 94.
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 (Slime mold).
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.DDB0215395; -.
DR PaxDb; Q55G10; -.
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; VYFPGSP; -.
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:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR11098; PTHR11098; 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; SSF51690; 1.
DR TIGRFAMs; TIGR01513; NAPRTase_put; 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
