PNCB_DANRE
ID PNCB_DANRE Reviewed; 546 AA.
AC Q6P3H4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
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; ORFNames=zgc:77870;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63987.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC063987; AAH63987.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q6P3H4; -.
DR SMR; Q6P3H4; -.
DR STRING; 7955.ENSDARP00000035128; -.
DR PaxDb; Q6P3H4; -.
DR ZFIN; ZDB-GENE-040426-1897; naprt.
DR eggNOG; KOG2511; Eukaryota.
DR InParanoid; Q6P3H4; -.
DR PhylomeDB; Q6P3H4; -.
DR Reactome; R-DRE-197264; Nicotinamide salvaging.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR UniPathway; UPA00253; UER00457.
DR PRO; PR:Q6P3H4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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; ISS:UniProtKB.
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: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..546
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000315684"
FT BINDING 22
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 209
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 316
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 378
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT MOD_RES 212
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P22253"
SQ SEQUENCE 546 AA; 59709 MW; 314B8D7B82A09E3D CRC64;
MATSNEAGSV LNRVPPLLTD LYQMAYAYWR AGRHNEPAVF ELFFRDNPFG GGFSLFAGLS
DCLLFLQNFS FSDDDVQYLR SVLPADTDAG FFSYLKELDC SCVSVSAVPE GSVVFARVPL
LEVSGPLAVV QLLETSLLCL VNYASLVCSN AARFRLAAGP RRRLMEMGLR RAQGPDGGLT
ASRYTYIGGF DLTSNALAGR LYGIPVAGTM AHSYITSFSS LEEVWPQTLK PCGGGDSIDF
ICLVKGLLGR VCQLLGSKTN LIREGELAAF LSYAIAYPQN FLPVIDSYSV RCSGLLCFCA
VALALFELQY RPLGVRLDSG DLCRQSLDVR RVFRECSKHF SVPQFESLII VGTNSISEQS
LSELNKKDNE IDVVGVGTHL VTCTRQPSLG CVYKLVEVRG RPRMKLSEDP EKSTLPGRKA
VYRLLDADGH PQMDVLCLCD EAAPAAGVEL QCFSLLGNST LQCSITPAQV SSLRTQVFSC
GQITLPLNSA SESRERAQIS LQMLNPYHKR LQEPHNYTVA LSERLHSLVS DIKKGNSKGS
NFLLSN
