IPT3_ARATH
ID IPT3_ARATH Reviewed; 336 AA.
AC Q93WC9; Q9LYB1;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Adenylate isopentenyltransferase 3, chloroplastic;
DE Short=AtIPT3;
DE EC=2.5.1.112;
DE AltName: Full=Adenylate dimethylallyltransferase 3;
DE AltName: Full=Cytokinin synthase 3;
DE Flags: Precursor;
GN Name=IPT3; OrderedLocusNames=At3g63110; ORFNames=T20O10.210;
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], FUNCTION, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=11313355; DOI=10.1074/jbc.m102130200;
RA Takei K., Sakakibara H., Sugiyama T.;
RT "Identification of genes encoding adenylate isopentenyltransferase, a
RT cytokinin biosynthesis enzyme, in Arabidopsis thaliana.";
RL J. Biol. Chem. 276:26405-26410(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11479373; DOI=10.1093/pcp/pce112;
RA Kakimoto T.;
RT "Identification of plant cytokinin biosynthetic enzymes as dimethylallyl
RT diphosphate:ATP/ADP isopentenyltransferases.";
RL Plant Cell Physiol. 42:677-685(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 SUBCELLULAR LOCATION.
RX PubMed=14726522; DOI=10.1074/jbc.m314195200;
RA Kasahara H., Takei K., Ueda N., Hishiyama S., Yamaya T., Kamiya Y.,
RA Yamaguchi S., Sakakibara H.;
RT "Distinct isoprenoid origins of cis- and trans-zeatin biosyntheses in
RT Arabidopsis.";
RL J. Biol. Chem. 279:14049-14054(2004).
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15356331; DOI=10.1093/pcp/pch119;
RA Takei K., Ueda N., Aoki K., Kuromori T., Hirayama T., Shinozaki K.,
RA Yamaya T., Sakakibara H.;
RT "AtIPT3 is a key determinant of nitrate-dependent cytokinin biosynthesis in
RT Arabidopsis.";
RL Plant Cell Physiol. 45:1053-1062(2004).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14675438; DOI=10.1046/j.1365-313x.2003.01945.x;
RA Miyawaki K., Matsumoto-Kitano M., Kakimoto T.;
RT "Expression of cytokinin biosynthetic isopentenyltransferase genes in
RT Arabidopsis: tissue specificity and regulation by auxin, cytokinin, and
RT nitrate.";
RL Plant J. 37:128-138(2004).
RN [9]
RP FUNCTION.
RX PubMed=15998742; DOI=10.1073/pnas.0500793102;
RA Sakakibara H., Kasahara H., Ueda N., Kojima M., Takei K., Hishiyama S.,
RA Asami T., Okada K., Kamiya Y., Yamaya T., Yamaguchi S.;
RT "Agrobacterium tumefaciens increases cytokinin production in plastids by
RT modifying the biosynthetic pathway in the host plant.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9972-9977(2005).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17062755; DOI=10.1073/pnas.0603522103;
RA Miyawaki K., Tarkowski P., Matsumoto-Kitano M., Kato T., Sato S.,
RA Tarkowska D., Tabata S., Sandberg G., Kakimoto T.;
RT "Roles of Arabidopsis ATP/ADP isopentenyltransferases and tRNA
RT isopentenyltransferases in cytokinin biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16598-16603(2006).
RN [11]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-333, AND ISOPRENYLATION AT
RP CYS-333.
RX PubMed=18184738; DOI=10.1104/pp.107.107425;
RA Galichet A., Hoyerova K., Kaminek M., Gruissem W.;
RT "Farnesylation directs AtIPT3 subcellular localization and modulates
RT cytokinin biosynthesis in Arabidopsis.";
RL Plant Physiol. 146:1155-1164(2008).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=19074290; DOI=10.1073/pnas.0805619105;
RA Matsumoto-Kitano M., Kusumoto T., Tarkowski P., Kinoshita-Tsujimura K.,
RA Vaclavikova K., Miyawaki K., Kakimoto T.;
RT "Cytokinins are central regulators of cambial activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20027-20031(2008).
CC -!- FUNCTION: Involved in cytokinin biosynthesis. Catalyzes the transfer of
CC an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP and
CC ADP. {ECO:0000269|PubMed:11313355, ECO:0000269|PubMed:15998742,
CC ECO:0000269|PubMed:17062755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + dimethylallyl diphosphate = diphosphate + N(6)-
CC (dimethylallyl)adenosine 5'-diphosphate; Xref=Rhea:RHEA:36327,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:73533,
CC ChEBI:CHEBI:456216; EC=2.5.1.112;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dimethylallyl diphosphate = diphosphate + N(6)-
CC (dimethylallyl)adenosine 5'-triphosphate; Xref=Rhea:RHEA:36331,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:73532; EC=2.5.1.112;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:14726522}. Nucleus membrane
CC {ECO:0000269|PubMed:18184738}; Lipid-anchor
CC {ECO:0000269|PubMed:18184738}. Cytoplasm {ECO:0000269|PubMed:18184738}.
CC Note=Farnesylation directs most of the protein to the nucleus/cytoplasm
CC despite the presence of a chloroplast transit peptide
CC (PubMed:18184738).
CC -!- TISSUE SPECIFICITY: Expressed the phloem companion cells.
CC {ECO:0000269|PubMed:14675438, ECO:0000269|PubMed:15356331}.
CC -!- INDUCTION: Down-regulated by cytokinins and up-regulated by nitrate,
CC but not by ammonium. {ECO:0000269|PubMed:14675438,
CC ECO:0000269|PubMed:15356331}.
CC -!- PTM: Farnesylated.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype except some decreased root
CC thickening, due the redundancy with other IPTs.
CC {ECO:0000269|PubMed:17062755, ECO:0000269|PubMed:19074290}.
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87756.1; Type=Erroneous initiation; Evidence={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; AB062610; BAB59043.1; -; mRNA.
DR EMBL; AB061401; BAB59030.1; -; mRNA.
DR EMBL; AL163816; CAB87756.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE80436.1; -; Genomic_DNA.
DR EMBL; AY125508; AAM78100.1; -; mRNA.
DR EMBL; BT001075; AAN46854.1; -; mRNA.
DR PIR; T48100; T48100.
DR RefSeq; NP_567138.1; NM_116176.3.
DR AlphaFoldDB; Q93WC9; -.
DR SMR; Q93WC9; -.
DR STRING; 3702.AT3G63110.1; -.
DR PaxDb; Q93WC9; -.
DR PRIDE; Q93WC9; -.
DR EnsemblPlants; AT3G63110.1; AT3G63110.1; AT3G63110.
DR GeneID; 825486; -.
DR Gramene; AT3G63110.1; AT3G63110.1; AT3G63110.
DR KEGG; ath:AT3G63110; -.
DR Araport; AT3G63110; -.
DR TAIR; locus:2099177; AT3G63110.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_4_1_1; -.
DR InParanoid; Q93WC9; -.
DR OMA; CGIPHHM; -.
DR OrthoDB; 1003231at2759; -.
DR PhylomeDB; Q93WC9; -.
DR BioCyc; ARA:AT3G63110-MON; -.
DR BioCyc; MetaCyc:AT3G63110-MON; -.
DR BRENDA; 2.5.1.112; 399.
DR PRO; PR:Q93WC9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93WC9; baseline and differential.
DR Genevisible; Q93WC9; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:UniProtKB.
DR GO; GO:0052623; F:ADP dimethylallyltransferase activity; ISS:TAIR.
DR GO; GO:0009824; F:AMP dimethylallyltransferase activity; IMP:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052622; F:ATP dimethylallyltransferase activity; ISS:TAIR.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central.
DR GO; GO:0009691; P:cytokinin biosynthetic process; IMP:TAIR.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR039657; Dimethylallyltransferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11088; PTHR11088; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Cytokinin biosynthesis; Cytoplasm; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Nucleus; Plastid; Prenylation;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..333
FT /note="Adenylate isopentenyltransferase 3, chloroplastic"
FT /id="PRO_0000391072"
FT PROPEP 334..336
FT /note="Removed in mature form"
FT /id="PRO_0000396781"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 333
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 333
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:18184738"
FT MUTAGEN 333
FT /note="C->S: Loss of farnesylation and decreased catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:18184738"
SQ SEQUENCE 336 AA; 37915 MW; 311440379FE6754E CRC64;
MIMKISMAMC KQPLPPSPTL DFPPARFGPN MLTLNPYGPK DKVVVIMGAT GTGKSRLSVD
IATRFRAEII NSDKIQVHQG LDIVTNKITS EESCGVPHHL LGVLPPEADL TAANYCHMAN
LSIESVLNRG KLPIIVGGSN SYVEALVDDK ENKFRSRYDC CFLWVDVALP VLHGFVSERV
DKMVESGMVE EVREFFDFSN SDYSRGIKKA IGFPEFDRFF RNEQFLNVED REELLSKVLE
EIKRNTFELA CRQREKIERL RKVKKWSIQR VDATPVFTKR RSKMDANVAW ERLVAGPSTD
TVSRFLLDIA SRRPLVEAST AVAAAMEREL SRCLVA
