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Database: UniProt
Entry: A0A0D3FR43_9ORYZ
LinkDB: A0A0D3FR43_9ORYZ
Original site: A0A0D3FR43_9ORYZ 
ID   A0A0D3FR43_9ORYZ        Unreviewed;       531 AA.
AC   A0A0D3FR43;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
OS   Oryza barthii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART03G40200.2};
RN   [1] {ECO:0000313|EnsemblPlants:OBART03G40200.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART03G40200.2};
RX   DOI=10.1007/s12284-009-9025-z;
RA   Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA   Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA   Knight J., Niazi F., Egholm M., Wing R.A.;
RT   "De novo next generation sequencing of plant genomes.";
RL   Rice 2:35-43(2009).
RN   [2] {ECO:0000313|EnsemblPlants:OBART03G40200.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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:0000256|ARBA:ARBA00023426}.
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:0000256|ARBA:ARBA00001240,
CC         ECO:0000256|RuleBase:RU365100};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
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:0000256|RuleBase:RU365100}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family.
CC       {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
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DR   AlphaFoldDB; A0A0D3FR43; -.
DR   EnsemblPlants; OBART03G40200.2; OBART03G40200.2; OBART03G40200.
DR   Gramene; OBART03G40200.2; OBART03G40200.2; OBART03G40200.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000026960; Chromosome 3.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
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; 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   NCBIfam; TIGR01513; NAPRTase_put; 1.
DR   PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 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; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR   SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365100};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|RuleBase:RU365100};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW   Transferase {ECO:0000256|RuleBase:RU365100}.
FT   DOMAIN          25..151
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          195..399
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          405..516
FT                   /note="Nicotinate phosphoribosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17956"
SQ   SEQUENCE   531 AA;  58949 MW;  4D70D52E0116DB8B CRC64;
     MAAAANGAGG GGGVPRPTNP MVTPLLTDLY QFTMAYAYWK AGKHLDRAVF DLYFRKNPFG
     GEFTIFGGLE ECIRFIANFK LTDTEITFLR SAMPTCEDGF FEYLSSIDCS DVEVYAIPEG
     SVVFPKVPLM IIEGPVAVIQ LLETPFLSLV NYASLVTTNA ARHRLVAGKS KNLLEFGLRR
     AQGPDGGISA SRYCYMGGFD ATSNVAAGRL FGIPIRGTHS HAFVSSFMGL DDIIDRTLAS
     SDGSNKCEDF VSLVQNWLAR IKDAGSLRGT FRETNLSELA AFTSYALAFP NSFLALVDTY
     DAAGIRLDSG DLAYLSVETR KFFRAIEEEF GFIGFGKMNI TASNDLNEET IDALNKQGHE
     VDAFGIGTYL VTCYAQAALG CVFKLVEINK QPRIKLSEDV SIPCKKRCYR LFGKEGYPLV
     DIMTGEDEPA PKVGERLLCR HPFNESKRAY VVPQHVEELL KCYWPGTSSE PREELPSINE
     IRSRCMGYLD RMRPDHMRRL NPTPYKVSVS AKLYDFIHFL WLNEAPVGEL Q
//
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