IPT7_ARATH
ID IPT7_ARATH Reviewed; 329 AA.
AC Q94ID1; Q8LA74; Q9LUG4;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Adenylate isopentenyltransferase 7, mitochondrial;
DE Short=AtIPT7;
DE EC=2.5.1.112;
DE AltName: Full=Adenylate dimethylallyltransferase 7;
DE AltName: Full=Cytokinin synthase 7;
DE Flags: Precursor;
GN Name=IPT7; OrderedLocusNames=At3g23630; ORFNames=MDB19.12;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [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.
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 [11]
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 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: Mitochondrion {ECO:0000269|PubMed:14726522}.
CC -!- TISSUE SPECIFICITY: Expressed in both the vascular stele and the phloem
CC companion cells of the root, in endodermis of the root elongation zone,
CC trichomes on young leaves, and some pollen tubes.
CC {ECO:0000269|PubMed:14675438, ECO:0000269|PubMed:15356331}.
CC -!- INDUCTION: Down-regulated by cytokinins and up-regulated by auxin.
CC {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; AB062613; BAB59046.1; -; mRNA.
DR EMBL; AB061405; BAB59033.1; -; mRNA.
DR EMBL; AB023036; BAB02782.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76788.1; -; Genomic_DNA.
DR EMBL; AY087990; AAM65536.1; -; mRNA.
DR EMBL; AK227296; BAE99312.1; -; mRNA.
DR RefSeq; NP_566735.1; NM_113267.3.
DR AlphaFoldDB; Q94ID1; -.
DR SMR; Q94ID1; -.
DR STRING; 3702.AT3G23630.1; -.
DR PaxDb; Q94ID1; -.
DR PRIDE; Q94ID1; -.
DR EnsemblPlants; AT3G23630.1; AT3G23630.1; AT3G23630.
DR GeneID; 821943; -.
DR Gramene; AT3G23630.1; AT3G23630.1; AT3G23630.
DR KEGG; ath:AT3G23630; -.
DR Araport; AT3G23630; -.
DR TAIR; locus:2088025; AT3G23630.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_4_1_1; -.
DR InParanoid; Q94ID1; -.
DR OMA; HEYLRNE; -.
DR OrthoDB; 1003231at2759; -.
DR PhylomeDB; Q94ID1; -.
DR BioCyc; ARA:AT3G23630-MON; -.
DR BioCyc; MetaCyc:AT3G23630-MON; -.
DR BRENDA; 2.5.1.112; 399.
DR PRO; PR:Q94ID1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94ID1; baseline and differential.
DR Genevisible; Q94ID1; AT.
DR GO; GO:0005739; C:mitochondrion; 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; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IEP: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 2: Evidence at transcript level;
KW ATP-binding; Cytokinin biosynthesis; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..329
FT /note="Adenylate isopentenyltransferase 7, mitochondrial"
FT /id="PRO_0000391075"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 37
FT /note="I -> V (in Ref. 2; BAB59033)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="G -> E (in Ref. 3; AAM65536)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="N -> K (in Ref. 3; AAM65536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 36980 MW; 66AFA61D3DE49AF8 CRC64;
MKFSISSLKQ VQPILCFKNK LSKVNVNSFL HPKEKVIFVM GATGSGKSRL AIDLATRFQG
EIINSDKIQL YKGLDVLTNK VTPKECRGVP HHLLGVFDSE AGNLTATQYS RLASQAISKL
SANNKLPIVA GGSNSYIEAL VNHSSGFLLN NYDCCFIWVD VSLPVLNSFV SKRVDRMMEA
GLLEEVREVF NPKANYSVGI RRAIGVPELH EYLRNESLVD RATKSKMLDV AVKNIKKNTE
ILACRQLKKI QRLHKKWKMS MHRVDATEVF LKRNVEEQDE AWENLVARPS ERIVDKFYNN
NNQLKNDDVE HCLAASYGGG SGSRAHNMI
