NPRT2_ARATH
ID NPRT2_ARATH Reviewed; 557 AA.
AC Q84WV8; O80459;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Nicotinate phosphoribosyltransferase 2 {ECO:0000303|PubMed:18978034};
DE EC=6.3.4.21 {ECO:0000250|UniProtKB:Q6XQN6};
GN Name=NAPRT2 {ECO:0000303|PubMed:18978034};
GN OrderedLocusNames=At2g23420 {ECO:0000312|Araport:AT2G23420};
GN ORFNames=F26B6.7 {ECO:0000312|EMBL:AAC23757.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:AAN71931.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=18978034; DOI=10.1105/tpc.107.056341;
RA Schippers J.H., Nunes-Nesi A., Apetrei R., Hille J., Fernie A.R.,
RA Dijkwel P.P.;
RT "The Arabidopsis onset of leaf death5 mutation of quinolinate synthase
RT affects nicotinamide adenine dinucleotide biosynthesis and causes early
RT ageing.";
RL Plant Cell 20:2909-2925(2008).
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 -!- INDUCTION: Up-regulated in the quinolinate synthase mutant old5 causing
CC increased NAD steady state levels. {ECO:0000269|PubMed:18978034}.
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=AAC23757.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC003040; AAC23757.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07453.1; -; Genomic_DNA.
DR EMBL; BT001932; AAN71931.1; -; mRNA.
DR PIR; T01131; T01131.
DR RefSeq; NP_179923.2; NM_127906.6.
DR AlphaFoldDB; Q84WV8; -.
DR SMR; Q84WV8; -.
DR IntAct; Q84WV8; 37.
DR STRING; 3702.AT2G23420.1; -.
DR iPTMnet; Q84WV8; -.
DR PaxDb; Q84WV8; -.
DR PRIDE; Q84WV8; -.
DR ProteomicsDB; 250596; -.
DR EnsemblPlants; AT2G23420.1; AT2G23420.1; AT2G23420.
DR GeneID; 816874; -.
DR Gramene; AT2G23420.1; AT2G23420.1; AT2G23420.
DR KEGG; ath:AT2G23420; -.
DR Araport; AT2G23420; -.
DR TAIR; locus:2046872; AT2G23420.
DR eggNOG; KOG2511; Eukaryota.
DR HOGENOM; CLU_025154_1_0_1; -.
DR InParanoid; Q84WV8; -.
DR OMA; VYFPGSP; -.
DR OrthoDB; 577034at2759; -.
DR PhylomeDB; Q84WV8; -.
DR BioCyc; ARA:AT2G23420-MON; -.
DR UniPathway; UPA00253; UER00457.
DR PRO; PR:Q84WV8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84WV8; baseline and differential.
DR Genevisible; Q84WV8; AT.
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; 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 PANTHER; PTHR11098; PTHR11098; 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; SSF51690; 1.
DR TIGRFAMs; TIGR01513; NAPRTase_put; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Ligase; Magnesium; Manganese; Metal-binding;
KW Phosphoprotein; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..557
FT /note="Nicotinate phosphoribosyltransferase 2"
FT /id="PRO_0000432218"
FT BINDING 31
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 219
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 329
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 391
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT MOD_RES 222
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P22253"
SQ SEQUENCE 557 AA; 62273 MW; F3F46DE14F3157F2 CRC64;
MEPKENGSEL GQKIIDGPTN PMVTPLLNDL YQFTMAYAYW KAGKHNERSV FDLYFRKNPF
GGEYTVFAGL EECVKFLANF KLTDEEIDFV QECLPGSEEA FCDYLRGLDC SDVEVYAIPE
GSVVFPKVPL MRVEGPVGVV QLLETPFLNL VNFASLVATN AARHRFVAGK SKSLLEFGAR
RAQGPDGAIS ASKYCYLGGF DATSNVAAGK LFGIPLRGTH SHAYVSSFMS TDEIVDKVLR
SADGKTTCED FVSHVQTWLK KIQYSPSLSG IFSETNQSEL AAFTSYALAF PKTFLALVDT
YDVMKSGIPN FCAVALALND FGYKALGIRL DSGDLAYLSR EARNFFCTVE RELKVPGFGK
MVVTASNDLN EETIDALNKQ GHEVDAFGIG TYLVTCYSQA ALGCVFKLVE INNQPRIKLS
EDVTKVSIPC KKRSYRLYGK EGYPLVDIMT GENEPPPKVG ERLLCRHPFN ESKRAYVVPQ
RVEELLKCYW RGSADEAREV LPPLKEIRDR CIKQLENMRP DHMRRLNPTP YKVSVSAKLY
DFIHFLWLNE APVGELQ
