IPT2_ARATH
ID IPT2_ARATH Reviewed; 466 AA.
AC Q9ZUX7; Q8RXJ9; Q9SQ59;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=tRNA dimethylallyltransferase 2;
DE EC=2.5.1.75;
DE AltName: Full=Isopentenyl-diphosphate: tRNA isopentenyltransferase 2;
DE Short=AtIPT2;
DE Short=IPP transferase 2;
DE Short=IPPT 2;
GN Name=IPT2; OrderedLocusNames=At2g27760; ORFNames=F15K20;
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 1), CATALYTIC ACTIVITY, AND GENE
RP 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] (ISOFORM 1), AND FUNCTION.
RX PubMed=11999372; DOI=10.1023/a:1014958816241;
RA Golovko A., Sitbon F., Tillberg E., Nicander B.;
RT "Identification of a tRNA isopentenyltransferase gene from Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 49:161-169(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORMS 1 AND 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 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CATALYTIC ACTIVITY, 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 [8]
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 [9]
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 [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).
CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the
CC adenine at position 37 in tRNAs that read codons beginning with
CC uridine, leading to the formation of N6-(dimethylallyl)adenosine
CC (i(6)A). Involved in the cis-type cytokinin biosynthesis.
CC {ECO:0000269|PubMed:11999372, ECO:0000269|PubMed:17062755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate =
CC diphosphate + N(6)-dimethylallyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74415; EC=2.5.1.75;
CC Evidence={ECO:0000269|PubMed:11313355, ECO:0000269|PubMed:11479373};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14726522}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZUX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZUX7-2; Sequence=VSP_038683, VSP_038684;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, with highest expression in
CC proliferating tissues. {ECO:0000269|PubMed:14675438}.
CC -!- INDUCTION: Not regulated by cytokinin, auxin or nitrate.
CC {ECO:0000269|PubMed:14675438}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due the redundancy with
CC IPT9. {ECO:0000269|PubMed:17062755}.
CC -!- MISCELLANEOUS: Contains 2 inserted regions when compared with other
CC members of the Arabidopsis IPT family. No adenylate
CC isopentenyltransferase activity detected neither in cv. Columbia, nor
CC in cv. Wassilewskija.
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR EMBL; AB062609; BAB59042.1; -; mRNA.
DR EMBL; AF109376; AAF00582.1; -; mRNA.
DR EMBL; AC005824; AAC73024.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08039.1; -; Genomic_DNA.
DR EMBL; AY080847; AAL87321.1; -; mRNA.
DR EMBL; BT001906; AAN71905.1; -; mRNA.
DR EMBL; AK221649; BAD95312.1; -; mRNA.
DR PIR; F84676; F84676.
DR PIR; T52061; T52061.
DR RefSeq; NP_565658.1; NM_128335.2. [Q9ZUX7-1]
DR AlphaFoldDB; Q9ZUX7; -.
DR SMR; Q9ZUX7; -.
DR STRING; 3702.AT2G27760.1; -.
DR PaxDb; Q9ZUX7; -.
DR PRIDE; Q9ZUX7; -.
DR ProteomicsDB; 248485; -. [Q9ZUX7-1]
DR EnsemblPlants; AT2G27760.1; AT2G27760.1; AT2G27760. [Q9ZUX7-1]
DR GeneID; 817322; -.
DR Gramene; AT2G27760.1; AT2G27760.1; AT2G27760. [Q9ZUX7-1]
DR KEGG; ath:AT2G27760; -.
DR Araport; AT2G27760; -.
DR TAIR; locus:2042103; AT2G27760.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_2_0_1; -.
DR InParanoid; Q9ZUX7; -.
DR OMA; NQFDQVE; -.
DR OrthoDB; 1003231at2759; -.
DR PhylomeDB; Q9ZUX7; -.
DR BioCyc; ARA:AT2G27760-MON; -.
DR BioCyc; MetaCyc:AT2G27760-MON; -.
DR BRENDA; 2.5.1.75; 399.
DR PRO; PR:Q9ZUX7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUX7; baseline and differential.
DR Genevisible; Q9ZUX7; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0009824; F:AMP dimethylallyltransferase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central.
DR GO; GO:0009691; P:cytokinin biosynthetic process; IDA:TAIR.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00185; IPP_trans; 1.
DR InterPro; IPR039657; Dimethylallyltransferase.
DR InterPro; IPR030666; IPP_transferase_euk.
DR InterPro; IPR018022; IPT.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11088; PTHR11088; 1.
DR PIRSF; PIRSF039110; IPP_transferase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00174; miaA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytokinin biosynthesis; Cytoplasm;
KW Magnesium; Nucleotide-binding; Reference proteome; Transferase;
KW tRNA processing.
FT CHAIN 1..466
FT /note="tRNA dimethylallyltransferase 2"
FT /id="PRO_0000391071"
FT REGION 52..55
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 433..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 29..34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 118
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.6"
FT /id="VSP_038683"
FT VAR_SEQ 137..150
FT /note="DTEECCADVASVVD -> MQQRIPRSVVQMLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.6"
FT /id="VSP_038684"
SQ SEQUENCE 466 AA; 53098 MW; FA95EADE815FBADA CRC64;
MMMLNPSNGG IEGEKMKKKA KVVVIMGPTG SGKSKLAVDL ASHFPVEIIN ADAMQIYSGL
DVLTNKVTVD EQKGVPHHLL GTVSSDMEFT ARDFRDFTVP LIEEIVSRNH IPVLVGGTHY
YIQAVVSKFL LDDAAEDTEE CCADVASVVD QDMVVESVFG RDDLSHGYEL LKELDPVAAN
RIHPNNHRKI NQYLSLHASR GVLPSKLYQG KTAENWGCIN ASRFDYCLIC MDAETAVLDR
YVEQRVDAMV DAGLLDEVYD IYKPGADYTR GLRQSIGVRE FEDFLKIHLS ETCAGHLTSL
SNDDKVMKEN LRKILNFPKD DKLRIMLEEA IDRVKLNTRR LLRRQKRRVS RLETVFGWNI
HYIDATEYIL SKSEESWNAQ VVKPASEIIR CFLETETESG RDPTSGKSIE RDLWTQYVCE
ACGNKILRGR HEWEHHKQGR THRKRTTRHK NSQTYKNREV QEAEVN
