APT2_ARATH
ID APT2_ARATH Reviewed; 192 AA.
AC Q42563; Q39004;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Adenine phosphoribosyltransferase 2;
DE Short=APRT 2;
DE Short=AtAPT2;
DE EC=2.4.2.7;
GN Name=APT2; OrderedLocusNames=At1g80050; ORFNames=F18B13.14;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8696367; DOI=10.1046/j.1365-313x.1996.9060891.x;
RA Schnorr K.M., Gaillard C., Biget E., Nygaard P., Laloue M.;
RT "A second form of adenine phosphoribosyltransferase in Arabidopsis thaliana
RT with relative specificity towards cytokinins.";
RL Plant J. 9:891-898(1996).
RN [2]
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 [3]
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 [4]
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 [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 CATALYTIC ACTIVITY.
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, ECO:0000269|PubMed:23658065};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for adenine (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC KM=330 uM for zeatin (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC KM=110 uM for isopentenyladenine (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC KM=15 uM for benzyladenine (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12010467};
CC Vmax=0.31 umol/min/mg enzyme with adenine as substrate (at pH 7.4 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:12010467};
CC Vmax=1 umol/min/mg enzyme with zeatin as substrate (at pH 7.4 and 37
CC degrees Celsius) {ECO:0000269|PubMed:12010467};
CC Vmax=0.36 umol/min/mg enzyme with isopentenyladenine as substrate (at
CC pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:12010467};
CC Vmax=0.1 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:0000305|PubMed:12010467}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; X96866; CAA65609.1; -; mRNA.
DR EMBL; X96867; CAA65610.1; -; Genomic_DNA.
DR EMBL; AC009322; AAD55485.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36351.1; -; Genomic_DNA.
DR EMBL; AY072021; AAL57714.1; -; mRNA.
DR EMBL; BT001122; AAN64513.1; -; mRNA.
DR PIR; S71272; S71272.
DR RefSeq; NP_178122.1; NM_106654.3.
DR AlphaFoldDB; Q42563; -.
DR SMR; Q42563; -.
DR BioGRID; 29563; 2.
DR IntAct; Q42563; 2.
DR STRING; 3702.AT1G80050.1; -.
DR PaxDb; Q42563; -.
DR PRIDE; Q42563; -.
DR ProteomicsDB; 246594; -.
DR EnsemblPlants; AT1G80050.1; AT1G80050.1; AT1G80050.
DR GeneID; 844345; -.
DR Gramene; AT1G80050.1; AT1G80050.1; AT1G80050.
DR KEGG; ath:AT1G80050; -.
DR Araport; AT1G80050; -.
DR TAIR; locus:2016309; AT1G80050.
DR eggNOG; KOG1712; Eukaryota.
DR HOGENOM; CLU_063339_0_3_1; -.
DR InParanoid; Q42563; -.
DR OMA; FKECTWL; -.
DR OrthoDB; 1291050at2759; -.
DR PhylomeDB; Q42563; -.
DR BioCyc; ARA:AT1G80050-MON; -.
DR UniPathway; UPA00588; UER00646.
DR PRO; PR:Q42563; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42563; baseline and differential.
DR Genevisible; Q42563; AT.
DR GO; GO:0005829; C:cytosol; ISS:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IDA:TAIR.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; ISS: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..192
FT /note="Adenine phosphoribosyltransferase 2"
FT /id="PRO_0000149515"
FT CONFLICT 40
FT /note="L -> M (in Ref. 1; CAA65610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21009 MW; 29D648EE59BBB026 CRC64;
MFAVENGLQG DPRLKAISDA IRVIPHFPKT GIMFQDITTL LLDPVAFKHV VDIFVDRYKH
MNISLVAGVE ARGFIFGPPI ALAIGAKFVP LRKPGKLPGR VISEEYELEY GRDCLEMSVE
AVKSEERALI IDDLVATGGT LSASINLLER AGAEVVECAC VVGLPKFKGQ CKLKGKPLYV
LVEPNQFDEL TL
