PNCB_DROME
ID PNCB_DROME Reviewed; 555 AA.
AC Q9VQX4; Q8MRQ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Nicotinate phosphoribosyltransferase;
DE Short=NAPRTase;
DE EC=6.3.4.21 {ECO:0000250|UniProtKB:Q6XQN6};
GN Name=Naprt {ECO:0000312|FlyBase:FBgn0031589};
GN ORFNames=CG3714 {ECO:0000312|FlyBase:FBgn0031589};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q9VQX4-1; Sequence=Displayed;
CC Name=2; Synonyms=C;
CC IsoId=Q9VQX4-2; Sequence=VSP_030614;
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; AE014134; AAF51037.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN11169.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11170.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11171.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11172.1; -; Genomic_DNA.
DR EMBL; AE014134; ABV53616.1; -; Genomic_DNA.
DR EMBL; AY119468; AAM50122.1; -; mRNA.
DR RefSeq; NP_001097077.1; NM_001103607.2. [Q9VQX4-2]
DR RefSeq; NP_608818.4; NM_134974.5. [Q9VQX4-2]
DR RefSeq; NP_722961.1; NM_164572.2. [Q9VQX4-1]
DR RefSeq; NP_722962.1; NM_164573.2. [Q9VQX4-2]
DR RefSeq; NP_722963.1; NM_164574.2. [Q9VQX4-2]
DR RefSeq; NP_722964.1; NM_164575.2. [Q9VQX4-2]
DR AlphaFoldDB; Q9VQX4; -.
DR SMR; Q9VQX4; -.
DR BioGRID; 59823; 1.
DR IntAct; Q9VQX4; 1.
DR PaxDb; Q9VQX4; -.
DR DNASU; 33626; -.
DR EnsemblMetazoa; FBtr0077479; FBpp0077168; FBgn0031589. [Q9VQX4-2]
DR EnsemblMetazoa; FBtr0077480; FBpp0077169; FBgn0031589. [Q9VQX4-2]
DR EnsemblMetazoa; FBtr0077481; FBpp0077170; FBgn0031589. [Q9VQX4-1]
DR EnsemblMetazoa; FBtr0077482; FBpp0077171; FBgn0031589. [Q9VQX4-2]
DR EnsemblMetazoa; FBtr0077483; FBpp0077172; FBgn0031589. [Q9VQX4-2]
DR EnsemblMetazoa; FBtr0113020; FBpp0111933; FBgn0031589. [Q9VQX4-2]
DR GeneID; 33626; -.
DR KEGG; dme:Dmel_CG3714; -.
DR UCSC; CG3714-RA; d. melanogaster. [Q9VQX4-1]
DR CTD; 93100; -.
DR FlyBase; FBgn0031589; Naprt.
DR VEuPathDB; VectorBase:FBgn0031589; -.
DR eggNOG; KOG2511; Eukaryota.
DR GeneTree; ENSGT00940000153456; -.
DR HOGENOM; CLU_025154_1_0_1; -.
DR InParanoid; Q9VQX4; -.
DR PhylomeDB; Q9VQX4; -.
DR Reactome; R-DME-197264; Nicotinamide salvaging.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR UniPathway; UPA00253; UER00457.
DR BioGRID-ORCS; 33626; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG3714; fly.
DR GenomeRNAi; 33626; -.
DR PRO; PR:Q9VQX4; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031589; Expressed in Malpighian tubule and 37 other tissues.
DR ExpressionAtlas; Q9VQX4; baseline and differential.
DR Genevisible; Q9VQX4; DM.
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; -; 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 Alternative splicing; Ligase; Magnesium; Manganese; Metal-binding;
KW Phosphoprotein; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..555
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000315686"
FT BINDING 33
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 180
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 222
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 225
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P22253"
FT VAR_SEQ 304
FT /note="K -> KSRETEQANTEPKHINDIKSENSPPKPKASPSTNGHQNGQGVGHVNG
FT HKTTNGHQNGSAQNNGSRTPKDTDIQDTSTSTTTTKTTATATGTLKTTTTVSNGTAYLP
FT KYVEKSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_030614"
SQ SEQUENCE 555 AA; 62165 MW; CA1E8C7954DD0F41 CRC64;
MNDRELGCAG GQFMDRGRMN QNGVVQPLLT DLYQITMAYA YWKSDKTDDT AVFDLFFRNN
PFHGEFTIFA GLEECLKFLD SFHYSQSDIE YLKQTLPEGI EHEFFEYLGN LTARDVTLYA
IDEGTVAFPR VPIIKIEGPL IIVQLLETTL LTLVNYASLM ATNAARYRMV AGKHVKLLEF
GLRRAQGPDG GLSASKYSYT GGFDGTSNVL AGKLFNIPVK GTHAHAYITS FSSIGELKTR
LIKHKQTGIL EDLLEHAVRH RALLSHLLDV STEESSEGEL AAMVSYAIAF PDGFMALVDT
YDVKRSGLLN FSAVALALND LGYHALGIRI DSGDLAYLSC LARETFEKVA ERFKVPWFNK
LTIVASNDIN EDTILSLNEQ GHKIDCFGIG THLVTCQRQP ALGCVYKLVE INGQPRIKLS
QDVEKVTMPG NKNAYRLYSA DGHALIDLLQ KVSEPPPAVG QKVLCRHPFQ ESKRAYVIPS
HVESLYKVYW KSGKICQQLP TLEQVREKVQ ISLKTLRNDH KRTLNPTPYK VAVSDNLYNF
IHDLWLQNAP IGELS
