ID   PNCB_RAT                Reviewed;         538 AA.
AC   Q6XQN1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-NOV-2023, entry version 107.
DE   RecName: Full=Nicotinate phosphoribosyltransferase;
DE            Short=NAPRTase;
DE            EC=6.3.4.21 {ECO:0000250|UniProtKB:Q6XQN6};
DE   AltName: Full=Nicotinate phosphoribosyltransferase domain-containing protein 1;
GN   Name=Naprt; Synonyms=Naprt1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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.
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   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6XQN6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
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; AY214330; AAP69608.1; -; mRNA.
DR   RefSeq; NP_997492.1; NM_207609.1.
DR   AlphaFoldDB; Q6XQN1; -.
DR   SMR; Q6XQN1; -.
DR   STRING; 10116.ENSRNOP00000010637; -.
DR   iPTMnet; Q6XQN1; -.
DR   PhosphoSitePlus; Q6XQN1; -.
DR   PaxDb; 10116-ENSRNOP00000010637; -.
DR   GeneID; 315085; -.
DR   KEGG; rno:315085; -.
DR   UCSC; RGD:1302945; rat.
DR   AGR; RGD:1302945; -.
DR   CTD; 93100; -.
DR   RGD; 1302945; Naprt.
DR   eggNOG; KOG2511; Eukaryota.
DR   InParanoid; Q6XQN1; -.
DR   OrthoDB; 1333333at2759; -.
DR   PhylomeDB; Q6XQN1; -.
DR   BRENDA; 6.3.4.21; 5301.
DR   Reactome; R-RNO-197264; Nicotinamide salvaging.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   UniPathway; UPA00253; UER00457.
DR   PRO; PR:Q6XQN1; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IDA:RGD.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009435; P:NAD biosynthetic process; IDA:RGD.
DR   GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR   CDD; cd01570; NAPRTase_A; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 2.
DR   InterPro; IPR013785; Aldolase_TIM.
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; 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   Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding; Phosphoprotein;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..538
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_0000315683"
FT   BINDING         21
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         210
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         318
FT                   /ligand="nicotinate"
FT                   /ligand_id="ChEBI:CHEBI:32544"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   BINDING         380
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT   MOD_RES         213
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P22253"
SQ   SEQUENCE   538 AA;  58565 MW;  0C68EF4A2C44D3D2 CRC64;
     MEMELDDQGR MVVRPLLTDL YQATMGLGYW RAGRACEEAE FELFFRHCPF GGSFALTAGL
     QDCIRFLRAF RLRDADVQFL ASVLPPDTDP AFFEHLRALD CSRVSVRALP EGSLAFPGVP
     LLQVSGPLLL VQLLETPLLC LVSYASLVAT NAARLRLIAG PDKRLLEMGL RRAQGPDGGF
     TASIYSYLGG FDSSSNTLAG QLRGVPVAGT LAHSFITSFL GSEVPPDPML APASSEGPAV
     DLPASVNLWL KHVCIYLGLE EREPHLGERA AFVAYALAFP RAFQGLLDSY SVRRSGLPNF
     LAVALALGEL GYRAVGVRLD SGDLLQQAKE IRGIFRTVGA EFQMPWLEFV PIAVSNNIDE
     KELARLAQKG SEVNVIGIGT NVVTCPKQPS MGCVYKLVSV GGQPRIKLTE ESQKETLPGS
     KAAFRFLVSE GSLLLDLLQL AEEPPPKAGQ ELRVWLQGAQ EPCTVKPAQV EPLLRLYLQQ
     GQPYEPLPSL EESRAFAQQS LSRLRPAHKQ LQNPAVYQVA LSEKLRALVD SLSARGAL
//