IPT8_ARATH
ID IPT8_ARATH Reviewed; 330 AA.
AC Q9LJL4;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Adenylate isopentenyltransferase 8, chloroplastic;
DE Short=AtIPT8;
DE EC=2.5.1.112;
DE AltName: Full=Adenylate dimethylallyltransferase 8;
DE AltName: Full=Cytokinin synthase 8;
DE AltName: Full=Plant growth activator 22;
DE Flags: Precursor;
GN Name=IPT8; Synonyms=PGA22; OrderedLocusNames=At3g19160; ORFNames=MVI11.16;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12529525; DOI=10.1104/pp.011494;
RA Sun J., Niu Q.W., Tarkowski P., Zheng B., Tarkowska D., Sandberg G.,
RA Chua N.H., Zuo J.;
RT "The Arabidopsis AtIPT8/PGA22 gene encodes an isopentenyl transferase that
RT is involved in de novo cytokinin biosynthesis.";
RL Plant Physiol. 131:167-176(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 DEVELOPMENTAL STAGE.
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: 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:12529525,
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}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and in immature seeds with
CC highest expression in the chalazal endosperm.
CC {ECO:0000269|PubMed:12529525, ECO:0000269|PubMed:14675438}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the early stages of embryo
CC development, up to the late heart stage. {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; AB062614; BAB59047.1; -; mRNA.
DR EMBL; AB061406; BAB59034.1; -; mRNA.
DR EMBL; AP000419; BAB02956.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76200.1; -; Genomic_DNA.
DR RefSeq; NP_188547.1; NM_112803.1.
DR AlphaFoldDB; Q9LJL4; -.
DR SMR; Q9LJL4; -.
DR STRING; 3702.AT3G19160.1; -.
DR PaxDb; Q9LJL4; -.
DR PRIDE; Q9LJL4; -.
DR EnsemblPlants; AT3G19160.1; AT3G19160.1; AT3G19160.
DR GeneID; 821450; -.
DR Gramene; AT3G19160.1; AT3G19160.1; AT3G19160.
DR KEGG; ath:AT3G19160; -.
DR Araport; AT3G19160; -.
DR TAIR; locus:2094128; AT3G19160.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_4_1_1; -.
DR InParanoid; Q9LJL4; -.
DR OMA; SSGWDIQ; -.
DR OrthoDB; 1003231at2759; -.
DR PhylomeDB; Q9LJL4; -.
DR BioCyc; ARA:AT3G19160-MON; -.
DR BioCyc; MetaCyc:AT3G19160-MON; -.
DR BRENDA; 2.5.1.112; 399.
DR PRO; PR:Q9LJL4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJL4; baseline and differential.
DR Genevisible; Q9LJL4; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052623; F:ADP dimethylallyltransferase activity; ISS:TAIR.
DR GO; GO:0009824; F:AMP dimethylallyltransferase activity; ISS: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; TAS: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; Chloroplast; Cytokinin biosynthesis; Nucleotide-binding;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..330
FT /note="Adenylate isopentenyltransferase 8, chloroplastic"
FT /id="PRO_0000391076"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 37322 MW; 4FEAD7F679317391 CRC64;
MQNLTSTFVS PSMIPITSPR LRLPPPRSVV PMTTVCMEQS YKQKVVVIMG ATGSGKSCLS
IDLATRFSGE IVNSDKIQFY DGLKVTTNQM SILERCGVPH HLLGELPPDD SELTTSEFRS
LASRSISEIT ARGNLPIIAG GSNSFIHALL VDRFDPKTYP FSSETSISSG LRYECCFLWV
DVSVSVLFEY LSKRVDQMME SGMFEELAGF YDPRYSGSAI RAHGIHKTIG IPEFDRYFSL
YPPERKQKMS EWDQARKGAY DEAVQEIKEN TWRLAKKQIE RIMKLKSSGW DIQRLDATPS
FGRSSREIWD NTVLDESIKV VKRFLVKDKV
