PNCB_BOVIN
ID PNCB_BOVIN Reviewed; 538 AA.
AC A5PK51; Q6XQN3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Nicotinate phosphoribosyltransferase;
DE Short=NAPRTase {ECO:0000250|UniProtKB:Q6XQN6};
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-538 (ISOFORM 1).
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 {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A5PK51-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A5PK51-2; Sequence=VSP_030609;
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; BC142357; AAI42358.1; -; mRNA.
DR EMBL; AY214328; AAP69606.1; -; mRNA.
DR RefSeq; NP_001092327.1; NM_001098857.2. [A5PK51-2]
DR AlphaFoldDB; A5PK51; -.
DR SMR; A5PK51; -.
DR STRING; 9913.ENSBTAP00000019496; -.
DR PaxDb; A5PK51; -.
DR PeptideAtlas; A5PK51; -.
DR PRIDE; A5PK51; -.
DR GeneID; 399559; -.
DR KEGG; bta:399559; -.
DR CTD; 93100; -.
DR eggNOG; KOG2511; Eukaryota.
DR InParanoid; A5PK51; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000009136; Unplaced.
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; 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 Alternative splicing; Cytoplasm; Ligase; Magnesium; Manganese;
KW Metal-binding; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..538
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000315680"
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"
FT VAR_SEQ 431..435
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030609"
FT CONFLICT 58
FT /note="A -> E (in Ref. 2; AAP69606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 57871 MW; CDE2E6FF34A613A9 CRC64;
MAAEQDPEGR AAARPLLTDL YQATMALGYW RAGRAQDQAE FELFFRQCPF GGAFALAAGL
RDCVRFLRAF RLRDADVQFL ASALPPDTDP AFFEHLRALD CSGVTVRALP EGSLAFPGVP
LLQVSGPLLV VQLLETPLLC LVSYASLIAT NAARLRLIAG PDKRLLEMGL RRAQGPDGGL
TASTYSYLGG FDASSNVLAG QLRGVPVAGT LAHSFVTSFS GSEVPPDPML APAAGQGSQV
DLAASVEMWL ERVCGHLGLG VQEPHRGERA AFVAYALAFP RAFQGLLDTY SVRRSGLPNF
LAVALALQEL GYQAVGVRLD SGDLLQQARE IRGVFRTAAA QFGVPWLQSV PIAVSNNIDE
EELARLAQKG SEVNVIGIGT SVVTCPRQPS LGCVYKLVSV GGQPRMKLTE DPEKQTLPGS
KAAFRLLGSD GSLLLDVLQL AEEPPPQAGQ ELRVWPRGAR ESRTVRPAHV EPLLRLWVQQ
GQLCEPLPSL AESRAFAQQS LHRLSPAHRR LEQPALYQVA LSEKLQALVD RLSARGAL
