APT3_ARATH
ID APT3_ARATH Reviewed; 183 AA.
AC Q9SUW2; Q8LG17;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Adenine phosphoribosyltransferase 3;
DE EC=2.4.2.7;
GN Name=APT3; OrderedLocusNames=At4g22570; ORFNames=F7K2.150;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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. May
CC contribute to the recycling of adenine into adenylate nucleotides and
CC the inactivation of cytokinins by phosphoribosylation. Possesses low
CC activity toward adenine and cytokinins. {ECO:0000269|PubMed:12010467,
CC ECO:0000269|PubMed:23658065}.
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};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for adenine (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC KM=76 uM for zeatin (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC KM=440 uM for isopentenyladenine (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC KM=370 uM for benzyladenine (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC Vmax=0.18 umol/min/mg enzyme with adenine as substrate (at pH 7.4 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:12010467};
CC Vmax=0.55 umol/min/mg enzyme with zeatin as substrate (at pH 7.4 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:12010467};
CC Vmax=1.6 umol/min/mg enzyme with isopentenyladenine as substrate (at
CC pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:12010467};
CC Vmax=0.27 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 7.4-7.5. {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: Cytoplasm {ECO:0000269|PubMed:12010467}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:23658065}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {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; AL033545; CAA22162.1; -; Genomic_DNA.
DR EMBL; AL161557; CAB79212.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84625.1; -; Genomic_DNA.
DR EMBL; BT002969; AAO22778.1; -; mRNA.
DR EMBL; BT004412; AAO42406.1; -; mRNA.
DR EMBL; AY084513; AAM61081.1; -; mRNA.
DR PIR; T05451; T05451.
DR RefSeq; NP_193988.1; NM_118383.4.
DR AlphaFoldDB; Q9SUW2; -.
DR SMR; Q9SUW2; -.
DR BioGRID; 13642; 3.
DR IntAct; Q9SUW2; 3.
DR STRING; 3702.AT4G22570.1; -.
DR PaxDb; Q9SUW2; -.
DR PRIDE; Q9SUW2; -.
DR ProteomicsDB; 244455; -.
DR EnsemblPlants; AT4G22570.1; AT4G22570.1; AT4G22570.
DR GeneID; 828353; -.
DR Gramene; AT4G22570.1; AT4G22570.1; AT4G22570.
DR KEGG; ath:AT4G22570; -.
DR Araport; AT4G22570; -.
DR TAIR; locus:2127480; AT4G22570.
DR eggNOG; KOG1712; Eukaryota.
DR HOGENOM; CLU_063339_0_3_1; -.
DR InParanoid; Q9SUW2; -.
DR OMA; KPGIVFR; -.
DR OrthoDB; 1291050at2759; -.
DR PhylomeDB; Q9SUW2; -.
DR BioCyc; ARA:AT4G22570-MON; -.
DR UniPathway; UPA00588; UER00646.
DR PRO; PR:Q9SUW2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUW2; baseline and differential.
DR Genevisible; Q9SUW2; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IDA:TAIR.
DR GO; GO:0006168; P:adenine salvage; TAS:TAIR.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
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 Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..183
FT /note="Adenine phosphoribosyltransferase 3"
FT /id="PRO_0000430130"
FT CONFLICT 126
FT /note="A -> S (in Ref. 4; AAM61081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 20352 MW; F46139F77E31D20B CRC64;
MSGNKEEEDP RIHGIKTKIR VVPDFPKKGI MFQDITTVLL DPKAFKDTID LFVERYRDKN
ISVVAGIEAR GFLFGPPIAL AIGAKFVPLR KPKKLPGETI FEEYELEYGN DRLEMHIGAV
EAGDRALVVD DLIATGGTLC AAINLLERVG AEVVECACVI ELPELKGRQR LKGKPLCMLV
EYR
