IPT1_ARATH
ID IPT1_ARATH Reviewed; 357 AA.
AC Q94ID3; Q9CA35;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Adenylate isopentenyltransferase 1, chloroplastic;
DE Short=AtIPT1;
DE EC=2.5.1.112 {ECO:0000269|PubMed:11313355, ECO:0000269|PubMed:15998742};
DE EC=2.5.1.27 {ECO:0000269|PubMed:15998742};
DE AltName: Full=Adenylate dimethylallyltransferase 1;
DE AltName: Full=Cytokinin synthase 1;
DE Flags: Precursor;
GN Name=IPT1; OrderedLocusNames=At1g68460; ORFNames=T26J14.3;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, 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 [3]
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 [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 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 [6]
RP TISSUE SPECIFICITY.
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 [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 BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
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 [9]
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: Involved in cytokinin biosynthesis. Catalyzes the transfer of
CC an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP, ADP
CC and AMP. Adenine, adenosine, isopentenylpyrophosphate and 1-hydroxy-2-
CC methyl-2-(E)-butenyl 4-diphosphate (HMBDP) are not used as substrates.
CC {ECO:0000269|PubMed:17062755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + dimethylallyl diphosphate = diphosphate + N(6)-
CC (dimethylallyl)adenosine 5'-phosphate; Xref=Rhea:RHEA:15285,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57526, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:456215; EC=2.5.1.27;
CC Evidence={ECO:0000269|PubMed:15998742};
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 Evidence={ECO:0000269|PubMed:11313355, ECO:0000269|PubMed:15998742};
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 Evidence={ECO:0000269|PubMed:11313355, ECO:0000269|PubMed:15998742};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=185 uM for ATP {ECO:0000269|PubMed:11313355,
CC ECO:0000269|PubMed:15998742};
CC KM=50 uM for DMAPP {ECO:0000269|PubMed:11313355,
CC ECO:0000269|PubMed:15998742};
CC pH dependence:
CC Optimum pH is 8.0. No activity at pH 6.0.
CC {ECO:0000269|PubMed:11313355, ECO:0000269|PubMed:15998742};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:14726522}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular stele of the roots, in
CC the xylem precursor cell files in the root tip, in leaf axils, ovules,
CC and immature seeds. {ECO:0000269|PubMed:14675438,
CC ECO:0000269|PubMed:15356331}.
CC -!- INDUCTION: Down-regulated by cytokinins. {ECO:0000269|PubMed:14675438}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due the redundancy with
CC other IPTs. {ECO:0000269|PubMed:17062755}.
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR EMBL; AB061400; BAB59029.1; -; mRNA.
DR EMBL; AB062607; BAB59040.1; -; mRNA.
DR EMBL; AC011915; AAG52395.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34796.1; -; Genomic_DNA.
DR PIR; F96708; F96708.
DR RefSeq; NP_177013.1; NM_105517.2.
DR AlphaFoldDB; Q94ID3; -.
DR SMR; Q94ID3; -.
DR STRING; 3702.AT1G68460.1; -.
DR PaxDb; Q94ID3; -.
DR PRIDE; Q94ID3; -.
DR ProteomicsDB; 248484; -.
DR EnsemblPlants; AT1G68460.1; AT1G68460.1; AT1G68460.
DR GeneID; 843175; -.
DR Gramene; AT1G68460.1; AT1G68460.1; AT1G68460.
DR KEGG; ath:AT1G68460; -.
DR Araport; AT1G68460; -.
DR TAIR; locus:2201292; AT1G68460.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_4_2_1; -.
DR InParanoid; Q94ID3; -.
DR OMA; RGVVHHL; -.
DR OrthoDB; 1003231at2759; -.
DR PhylomeDB; Q94ID3; -.
DR BioCyc; ARA:AT1G68460-MON; -.
DR BioCyc; MetaCyc:AT1G68460-MON; -.
DR BRENDA; 2.5.1.112; 399.
DR BRENDA; 2.5.1.27; 399.
DR SABIO-RK; Q94ID3; -.
DR PRO; PR:Q94ID3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94ID3; baseline and differential.
DR Genevisible; Q94ID3; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; IDA:UniProtKB.
DR GO; GO:0052623; F:ADP dimethylallyltransferase activity; IDA:TAIR.
DR GO; GO:0009824; F:AMP dimethylallyltransferase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052622; F:ATP dimethylallyltransferase activity; IDA:TAIR.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central.
DR GO; GO:0009691; P:cytokinin biosynthetic process; TAS:TAIR.
DR GO; GO:0080117; P:secondary growth; IGI: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; Nucleotide-binding;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..71
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 72..357
FT /note="Adenylate isopentenyltransferase 1, chloroplastic"
FT /id="PRO_0000391070"
FT REGION 20..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 337
FT /note="N -> I (in Ref. 1; BAB59029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40765 MW; 8F37C63A3BE3ED2D CRC64;
MTELNFHLLP IISDRFTTTT TTSPSFSSHS SSSSSLLSFT KRRRKHQPLV SSIRMEQSRS
RNRKDKVVVI LGATGAGKSR LSVDLATRFP SEIINSDKIQ VYEGLEITTN QITLQDRRGV
PHHLLGVINP EHGELTAGEF RSAASNVVKE ITSRQKVPII AGGSNSFVHA LLAQRFDPKF
DPFSSGSCLI SSDLRYECCF IWVDVSETVL YEYLLRRVDE MMDSGMFEEL SRFYDPVKSG
LETRFGIRKA IGVPEFDGYF KEYPPEKKMI KWDALRKAAY DKAVDDIKRN TWTLAKRQVK
KIEMLKDAGW EIERVDATAS FKAVMMKSSS EKKWRENWEE QVLEPSVKIV KRHLVQN
