PNCB_RAT
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 03-AUG-2022, entry version 102.
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; Q6XQN1; -.
DR PRIDE; Q6XQN1; -.
DR GeneID; 315085; -.
DR KEGG; rno:315085; -.
DR UCSC; RGD:1302945; rat.
DR CTD; 93100; -.
DR RGD; 1302945; Naprt.
DR eggNOG; KOG2511; Eukaryota.
DR InParanoid; Q6XQN1; -.
DR OrthoDB; 577034at2759; -.
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:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
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 Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR11098; PTHR11098; 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 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
