APT1_ARATH
ID APT1_ARATH Reviewed; 243 AA.
AC P31166; Q8LGF6; Q9FZJ0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Adenine phosphoribosyltransferase 1, chloroplastic;
DE Short=APRT 1;
DE Short=AtAPT1;
DE EC=2.4.2.7;
DE Flags: Precursor;
GN Name=APT1; Synonyms=APT; OrderedLocusNames=At1g27450; ORFNames=F17L21.24;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=1558943; DOI=10.1007/bf00020008;
RA Moffatt B.A., McWhinnie E.A., Burkhart W.E., Pasternak J.J.,
RA Rothstein S.J.;
RT "A complete cDNA for adenine phosphoribosyltransferase from Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 18:653-662(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=8206375; DOI=10.1016/0378-1119(94)90098-1;
RA Moffatt B.A., McWhinnie E.A., Agarwal S.K., Schaff D.A.;
RT "The adenine phosphoribosyltransferase-encoding gene of Arabidopsis
RT thaliana.";
RL Gene 143:211-216(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9520269; DOI=10.1007/s004380050656;
RA Gaillard C., Moffatt B.A., Blacker M., Laloue M.;
RT "Male sterility associated with APRT deficiency in Arabidopsis thaliana
RT results from a mutation in the gene APT1.";
RL Mol. Gen. Genet. 257:348-353(1998).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12010467; DOI=10.1034/j.1399-3054.2002.1150106.x;
RA Allen M., Qin W., Moreau F., Moffatt B.;
RT "Adenine phosphoribosyltransferase isoforms of Arabidopsis and their
RT potential contributions to adenine and cytokinin metabolism.";
RL Physiol. Plantarum 115:56-68(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP FUNCTION.
RX PubMed=22859732; DOI=10.1093/mp/sss065;
RA Sukrong S., Yun K.Y., Stadler P., Kumar C., Facciuolo T., Moffatt B.A.,
RA Falcone D.L.;
RT "Improved growth and stress tolerance in the Arabidopsis oxt1 mutant
RT triggered by altered adenine metabolism.";
RL Mol. Plant 5:1310-1332(2012).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PRO-85; LEU-99; ARG-149; GLY-168; GLY-195 AND GLY-195.
RX PubMed=23658065; DOI=10.1093/mp/sst071;
RA Zhang X., Chen Y., Lin X., Hong X., Zhu Y., Li W., He W., An F., Guo H.;
RT "Adenine phosphoribosyl transferase 1 is a key enzyme catalyzing cytokinin
RT conversion from nucleobases to nucleotides in Arabidopsis.";
RL Mol. Plant 6:1661-1672(2013).
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC Contributes primarily to the recycling of adenine into adenylate
CC nucleotides, but is also involved in the inactivation of cytokinins by
CC phosphoribosylation. Catalyzes the conversion of cytokinins from free
CC bases (active form) to the corresponding nucleotides (inactive form).
CC {ECO:0000269|PubMed:12010467, ECO:0000269|PubMed:22859732,
CC ECO:0000269|PubMed:23658065, ECO:0000269|PubMed:9520269}.
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 Evidence={ECO:0000269|PubMed:12010467, ECO:0000269|PubMed:23658065};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for adenine (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC KM=1800 uM for zeatin (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC KM=2500 uM for isopentenyladenine (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC KM=2400 uM for benzyladenine (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC Vmax=9.6 umol/min/mg enzyme with adenine as substrate (at pH 7.4 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:12010467};
CC Vmax=10 umol/min/mg enzyme with zeatin as substrate (at pH 7.4 and 37
CC degrees Celsius) {ECO:0000269|PubMed:12010467};
CC Vmax=6.7 umol/min/mg enzyme with isopentenyladenine as substrate (at
CC pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:12010467};
CC Vmax=1.5 umol/min/mg enzyme with benzyladenine as substrate (at pH
CC 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:12010467};
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:12010467};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P31166-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31166-2; Sequence=VSP_009002;
CC -!- DISRUPTION PHENOTYPE: Male sterility due to pollen abortion after
CC meiosis. Accumulation of free bases of cytokinins and enhanced
CC resistance to exogenous cytokinins. {ECO:0000269|PubMed:23658065,
CC ECO:0000269|PubMed:9520269}.
CC -!- MISCELLANEOUS: Plants with reduced activity of APT1 and increased
CC levels of cellular adenine show enhanced stress tolerance and improve
CC growth, leading to increases in plant biomass.
CC {ECO:0000305|PubMed:22859732}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99737.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X58640; CAA41497.1; -; mRNA.
DR EMBL; L19637; AAA20677.1; -; Genomic_DNA.
DR EMBL; AC004557; AAF99737.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30831.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30832.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60751.1; -; Genomic_DNA.
DR EMBL; AF325045; AAG40397.1; -; mRNA.
DR EMBL; AY128377; AAM91580.1; -; mRNA.
DR EMBL; BT000370; AAN15689.1; -; mRNA.
DR EMBL; AY084300; AAM60891.1; -; mRNA.
DR PIR; G86399; G86399.
DR PIR; S20867; S20867.
DR RefSeq; NP_001323015.1; NM_001332762.1. [P31166-2]
DR RefSeq; NP_564284.1; NM_102509.4. [P31166-1]
DR RefSeq; NP_849714.1; NM_179383.3. [P31166-2]
DR AlphaFoldDB; P31166; -.
DR SMR; P31166; -.
DR BioGRID; 24871; 3.
DR IntAct; P31166; 4.
DR MetOSite; P31166; -.
DR PRIDE; P31166; -.
DR ProteomicsDB; 244487; -. [P31166-1]
DR EnsemblPlants; AT1G27450.1; AT1G27450.1; AT1G27450. [P31166-1]
DR EnsemblPlants; AT1G27450.2; AT1G27450.2; AT1G27450. [P31166-2]
DR EnsemblPlants; AT1G27450.4; AT1G27450.4; AT1G27450. [P31166-2]
DR GeneID; 839636; -.
DR Gramene; AT1G27450.1; AT1G27450.1; AT1G27450. [P31166-1]
DR Gramene; AT1G27450.2; AT1G27450.2; AT1G27450. [P31166-2]
DR Gramene; AT1G27450.4; AT1G27450.4; AT1G27450. [P31166-2]
DR KEGG; ath:AT1G27450; -.
DR Araport; AT1G27450; -.
DR InParanoid; P31166; -.
DR PhylomeDB; P31166; -.
DR BioCyc; MetaCyc:AT1G27450-MON; -.
DR UniPathway; UPA00588; UER00646.
DR PRO; PR:P31166; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P31166; baseline and differential.
DR Genevisible; P31166; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006168; P:adenine salvage; IEA:InterPro.
DR GO; GO:0044209; P:AMP salvage; TAS:UniProtKB.
DR GO; GO:0009690; P:cytokinin metabolic process; IMP:UniProtKB.
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 TIGRFAMs; TIGR01090; apt; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chloroplast; Cytoplasm;
KW Glycosyltransferase; Plastid; Purine salvage; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..243
FT /note="Adenine phosphoribosyltransferase 1, chloroplastic"
FT /id="PRO_0000149514"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:1558943"
FT /id="VSP_009002"
FT MUTAGEN 85
FT /note="P->T: In apt1-5; loss of activity."
FT /evidence="ECO:0000269|PubMed:23658065"
FT MUTAGEN 99
FT /note="L->F: In apt1-6; reduces activity 10-fold."
FT /evidence="ECO:0000269|PubMed:23658065"
FT MUTAGEN 149
FT /note="R->K: In apt1-7; loss of activity and male
FT sterility."
FT /evidence="ECO:0000269|PubMed:23658065"
FT MUTAGEN 168
FT /note="G->E: In apt1-4; reduces activity 3-fold."
FT /evidence="ECO:0000269|PubMed:23658065"
FT MUTAGEN 195
FT /note="G->D: In apt1-8; loss of activity and male
FT sterility."
FT /evidence="ECO:0000269|PubMed:23658065"
FT MUTAGEN 196
FT /note="G->R: In apt1-9; loss of activity and male
FT sterility."
FT INIT_MET P31166-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES P31166-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 243 AA; 26396 MW; 92ABF089CA66C0FD CRC64;
MQTIIISPLV SHRLCLARAV PCNRLLNNHH RAPPSIRLSN HRSTTSLRLF SSAAASRDSE
MATEDVQDPR IAKIASSIRV IPDFPKPGIM FQDITTLLLD TEAFKDTIAL FVDRYKDKGI
SVVAGVEARG FIFGPPIALA IGAKFVPMRK PKKLPGKVIS EEYSLEYGTD TIEMHVGAVE
PGERAIIIDD LIATGGTLAA AIRLLERVGV KIVECACVIE LPELKGKEKL GETSLFVLVK
SAA
