IPT9_ARATH
ID IPT9_ARATH Reviewed; 463 AA.
AC Q9C5J6; Q8LDP3; Q94IC8;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=tRNA dimethylallyltransferase 9;
DE EC=2.5.1.75;
DE AltName: Full=Isopentenyl-diphosphate: tRNA isopentenyltransferase 9;
DE Short=AtIPT9;
DE Short=IPP transferase 9;
DE Short=IPPT 9;
GN Name=IPT9; OrderedLocusNames=At5g20040; ORFNames=F28I16.190;
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 2), 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 [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 [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] (ISOFORM 1).
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 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 [6]
RP 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 [7]
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 [8]
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:11313355, 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C5J6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5J6-2; Sequence=VSP_038685;
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 IPT2. Often chlorotic. {ECO:0000269|PubMed:17062755}.
CC -!- SIMILARITY: Belongs to the IPP transferase 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; AB062615; BAB59048.1; -; mRNA.
DR EMBL; AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92782.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92783.1; -; Genomic_DNA.
DR EMBL; AF360208; AAK25918.1; -; mRNA.
DR EMBL; AY040056; AAK64114.1; -; mRNA.
DR EMBL; AY085878; AAM63091.1; -; mRNA.
DR RefSeq; NP_568390.2; NM_122011.4. [Q9C5J6-2]
DR RefSeq; NP_851043.1; NM_180712.3. [Q9C5J6-1]
DR AlphaFoldDB; Q9C5J6; -.
DR SMR; Q9C5J6; -.
DR STRING; 3702.AT5G20040.3; -.
DR PaxDb; Q9C5J6; -.
DR PRIDE; Q9C5J6; -.
DR ProteomicsDB; 247041; -. [Q9C5J6-1]
DR EnsemblPlants; AT5G20040.1; AT5G20040.1; AT5G20040. [Q9C5J6-1]
DR EnsemblPlants; AT5G20040.2; AT5G20040.2; AT5G20040. [Q9C5J6-2]
DR GeneID; 832126; -.
DR Gramene; AT5G20040.1; AT5G20040.1; AT5G20040. [Q9C5J6-1]
DR Gramene; AT5G20040.2; AT5G20040.2; AT5G20040. [Q9C5J6-2]
DR KEGG; ath:AT5G20040; -.
DR Araport; AT5G20040; -.
DR eggNOG; KOG1384; Eukaryota.
DR InParanoid; Q9C5J6; -.
DR OMA; NFVYDAY; -.
DR PhylomeDB; Q9C5J6; -.
DR BioCyc; ARA:AT5G20040-MON; -.
DR PRO; PR:Q9C5J6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5J6; baseline and differential.
DR Genevisible; Q9C5J6; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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; IPR018022; IPT.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11088; PTHR11088; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00174; miaA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytokinin biosynthesis; Cytoplasm;
KW Magnesium; Nucleotide-binding; Reference proteome; Transferase;
KW tRNA processing.
FT CHAIN 1..463
FT /note="tRNA dimethylallyltransferase 9"
FT /id="PRO_0000391077"
FT REGION 82..85
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT BINDING 57..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 59..64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 148
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 431..434
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11313355"
FT /id="VSP_038685"
FT CONFLICT 121
FT /note="V -> L (in Ref. 5; AAM63091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 52264 MW; A36E0736B56DF50C CRC64;
MVIGSGVFLT RTCYLRLQPP SLVLRRRFCA ATTACSVPLN GNKKKKSEKE KVIVISGPTG
AGKSRLAMEL AKRLNGEIIS ADSVQVYKGL DVGSAKPSDS DRKVVPHHLI DILHPSQDYS
VGQFYDDGRQ ATKDILNRGR VPIVTGGTGL YLRWFMYGKP DVPKPSPEVI AEAHDMLVGF
QTEYNWDAAV ELVVNAGDPK ASSLPRNDWY RLRRSLEILK STGSPPSSFR IPYDSFRVNL
VAPDADDFLE DGSSADISIQ NIETDLDYDF LCFFLSSPRV ALYRSIDFRC EDMLSGPNGV
LSEARWLLDL GLLPNSNPAT RAIGYRQAME YLLQCRRYEG ESSPREFYAF LNKFQTASRN
FAKRQMTWFR CEPMYHWLNA SKPLDSILQC IYDAYESEAE MVEIPESLRM SKDVRDSREA
SELKGYRSKN RHFVRREDCS SVLEWIRSEG CKSEASCVES AIA
