APT_DROME
ID APT_DROME Reviewed; 182 AA.
AC P12426; Q9W069;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Adenine phosphoribosyltransferase;
DE Short=APRT;
DE EC=2.4.2.7;
GN Name=Aprt; ORFNames=CG18315;
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 [MRNA].
RX PubMed=3125085; DOI=10.1016/0378-1119(87)90268-x;
RA Johnson D.H., Edstroem J.-E., Burnett J.B., Friedman T.B.;
RT "Cloning of a Drosophila melanogaster adenine phosphoribosyltransferase
RT structural gene and deduced amino acid sequence of the enzyme.";
RL Gene 59:77-86(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8492806; DOI=10.1007/bf00291997;
RA Johnson D.H.;
RT "Adenine phosphoribosyltransferase genes in two Drosophila species: dosage
RT compensation, a nuclear matrix attachment site, and a novel intron
RT position.";
RL Mol. Gen. Genet. 238:383-389(1993).
RN [3]
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 [4]
RP GENOME REANNOTATION.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
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 a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate +
CC adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7;
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; M18432; AAA28377.1; -; mRNA.
DR EMBL; L06280; AAA57204.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47589.1; -; Genomic_DNA.
DR EMBL; AY119066; AAM50926.1; -; mRNA.
DR PIR; A29596; A29596.
DR PIR; S34831; S34831.
DR RefSeq; NP_001286908.1; NM_001299979.1.
DR RefSeq; NP_001286909.1; NM_001299980.1.
DR RefSeq; NP_476637.1; NM_057289.3.
DR AlphaFoldDB; P12426; -.
DR SMR; P12426; -.
DR BioGRID; 71230; 7.
DR DIP; DIP-22863N; -.
DR IntAct; P12426; 1.
DR STRING; 7227.FBpp0088438; -.
DR PaxDb; P12426; -.
DR PRIDE; P12426; -.
DR DNASU; 48224; -.
DR EnsemblMetazoa; FBtr0089420; FBpp0088438; FBgn0000109.
DR EnsemblMetazoa; FBtr0346440; FBpp0312098; FBgn0000109.
DR EnsemblMetazoa; FBtr0346441; FBpp0312099; FBgn0000109.
DR GeneID; 48224; -.
DR KEGG; dme:Dmel_CG18315; -.
DR CTD; 353; -.
DR FlyBase; FBgn0000109; Aprt.
DR VEuPathDB; VectorBase:FBgn0000109; -.
DR eggNOG; KOG1712; Eukaryota.
DR HOGENOM; CLU_063339_3_2_1; -.
DR InParanoid; P12426; -.
DR OMA; KPGIVFR; -.
DR OrthoDB; 1291050at2759; -.
DR PhylomeDB; P12426; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-74217; Purine salvage.
DR UniPathway; UPA00588; UER00646.
DR BioGRID-ORCS; 48224; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 48224; -.
DR PRO; PR:P12426; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000109; Expressed in adult Malpighian tubule (Drosophila) and 23 other tissues.
DR ExpressionAtlas; P12426; baseline and differential.
DR Genevisible; P12426; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0002055; F:adenine binding; IBA:GO_Central.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0006168; P:adenine salvage; IBA:GO_Central.
DR GO; GO:0044209; P:AMP salvage; IBA:GO_Central.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR InterPro; IPR005764; Ade_phspho_trans.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..182
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149512"
FT CONFLICT 64
FT /note="V -> I (in Ref. 1; AAA28377 and 2; AAA57204)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="I -> S (in Ref. 1; AAA28377 and 2; AAA57204)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="G -> R (in Ref. 1; AAA28377 and 2; AAA57204)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="V -> VV (in Ref. 1; AAA28377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 19690 MW; E69C129905AE4745 CRC64;
MSPSISAEDK LDYVKSKIGE YPNFPKEGIL FRDIFGALTD PKACVYLRDL LVDHIRESAP
EAEVIVGLDS RGFLFNLLIA TELGLGCAPI RKKGKLAGEV VSVEYKLEYG IDTFELQKSA
IKPGQKVVVV DDLLATGGSL VAATELIGKV GGVVVESLVV MELVGLEGRK RLDGKVHSLI
KY
