APT5_ARATH
ID APT5_ARATH Reviewed; 191 AA.
AC Q9LFP0;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Adenine phosphoribosyltransferase 5;
DE Short=AtAPT5;
DE EC=2.4.2.7;
GN Name=APT5; OrderedLocusNames=At5g11160; ORFNames=F2I11.50;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 FUNCTION, CATALYTIC ACTIVITY, 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, but can efficiently convert cytokinins from
CC free bases (active form) to the corresponding nucleotides (inactive
CC form). {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:23658065};
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}.
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}.
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DR EMBL; AL360314; CAB96651.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91640.1; -; Genomic_DNA.
DR EMBL; BT004028; AAO42064.1; -; mRNA.
DR EMBL; BT005077; AAO50610.1; -; mRNA.
DR RefSeq; NP_196677.1; NM_121154.4.
DR AlphaFoldDB; Q9LFP0; -.
DR SMR; Q9LFP0; -.
DR BioGRID; 16263; 3.
DR IntAct; Q9LFP0; 3.
DR STRING; 3702.AT5G11160.1; -.
DR PaxDb; Q9LFP0; -.
DR PRIDE; Q9LFP0; -.
DR ProteomicsDB; 240610; -.
DR EnsemblPlants; AT5G11160.1; AT5G11160.1; AT5G11160.
DR GeneID; 830985; -.
DR Gramene; AT5G11160.1; AT5G11160.1; AT5G11160.
DR KEGG; ath:AT5G11160; -.
DR Araport; AT5G11160; -.
DR TAIR; locus:2147967; AT5G11160.
DR eggNOG; KOG1712; Eukaryota.
DR HOGENOM; CLU_063339_0_3_1; -.
DR InParanoid; Q9LFP0; -.
DR OMA; ISLMSEY; -.
DR OrthoDB; 1291050at2759; -.
DR PhylomeDB; Q9LFP0; -.
DR BioCyc; ARA:AT5G11160-MON; -.
DR BRENDA; 2.4.2.7; 399.
DR UniPathway; UPA00588; UER00646.
DR PRO; PR:Q9LFP0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFP0; baseline and differential.
DR Genevisible; Q9LFP0; AT.
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; 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..191
FT /note="Adenine phosphoribosyltransferase 5"
FT /id="PRO_0000430132"
SQ SEQUENCE 191 AA; 20757 MW; EC202C6FBD858E78 CRC64;
MFAAENGLKG DPRLEAISAA IRVVPNFPKK GIMFQDITTL LLDHKAFKHT IDIFVDRYKD
MQISVVAGVE ARGFLFGPSI ALAIGAKFIP LRKPGKLPGK VISESYELEY GHDRLEMHVG
AVEPRERVII IDDLVATGGT LSAAMSLLES QGAEVVECAC VIGLPEVKGQ HKLKGKPLYV
LVEPSGLDEF C
