IPT4_ARATH
ID IPT4_ARATH Reviewed; 318 AA.
AC Q9SB60;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Adenylate isopentenyltransferase 4;
DE Short=AtIPT4;
DE EC=2.5.1.112;
DE AltName: Full=Adenylate dimethylallyltransferase 4;
DE AltName: Full=Cytokinin synthase 4;
GN Name=IPT4; OrderedLocusNames=At4g24650; ORFNames=F22K18.150;
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. 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], BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
RP 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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, 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 [7]
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 [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, but not to AMP. Has no DMAPP:tRNA isopentenyltransferase activity.
CC {ECO:0000269|PubMed:15998742, 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 Evidence={ECO:0000269|PubMed:11479373};
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:11479373};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for ATP {ECO:0000269|PubMed:11479373};
CC KM=6.5 uM for DMAPP {ECO:0000269|PubMed:11479373};
CC Vmax=0.22 umol/min/mg enzyme {ECO:0000269|PubMed:11479373};
CC -!- INTERACTION:
CC Q9SB60; Q9SLH3: RGA; NbExp=3; IntAct=EBI-25522816, EBI-963624;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14726522}.
CC -!- TISSUE SPECIFICITY: Expressed in immature seeds with highest expression
CC in the chalazal endosperm. {ECO:0000269|PubMed:14675438}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the early stages of embryo
CC development, up to the early heart stage.
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; AB062611; BAB59044.1; -; mRNA.
DR EMBL; AB061402; BAB59031.1; -; mRNA.
DR EMBL; AL035356; CAA22998.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79375.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84938.1; -; Genomic_DNA.
DR PIR; T05569; T05569.
DR RefSeq; NP_194196.1; NM_118598.1.
DR AlphaFoldDB; Q9SB60; -.
DR SMR; Q9SB60; -.
DR BioGRID; 13856; 1.
DR IntAct; Q9SB60; 1.
DR STRING; 3702.AT4G24650.1; -.
DR PaxDb; Q9SB60; -.
DR PRIDE; Q9SB60; -.
DR EnsemblPlants; AT4G24650.1; AT4G24650.1; AT4G24650.
DR GeneID; 828567; -.
DR Gramene; AT4G24650.1; AT4G24650.1; AT4G24650.
DR KEGG; ath:AT4G24650; -.
DR Araport; AT4G24650; -.
DR TAIR; locus:2121979; AT4G24650.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_4_1_1; -.
DR InParanoid; Q9SB60; -.
DR OMA; ESACWER; -.
DR OrthoDB; 1003231at2759; -.
DR PhylomeDB; Q9SB60; -.
DR BioCyc; ARA:AT4G24650-MON; -.
DR BioCyc; MetaCyc:AT4G24650-MON; -.
DR BRENDA; 2.5.1.112; 399.
DR PRO; PR:Q9SB60; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB60; baseline and differential.
DR Genevisible; Q9SB60; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052623; F:ADP dimethylallyltransferase activity; IDA: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; IDA:TAIR.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central.
DR GO; GO:0009691; P:cytokinin biosynthetic process; IMP: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; IPR018022; IPT.
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; Cytokinin biosynthesis; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..318
FT /note="Adenylate isopentenyltransferase 4"
FT /id="PRO_0000391069"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 318 AA; 36674 MW; BE8BD9FF52E20F08 CRC64;
MKCNDKMVVI MGATGSGKSS LSVDLALHFK AEIINSDKMQ FYDGLKITTN QSTIEDRRGV
PHHLLGELNP EAGEVTAAEF RVMAAEAISE ITQRKKLPIL AGGSNSYIHA LLAKSYDPEN
YPFSDHKGSI CSELKYDCCF IWIDVDQSVL FEYLSLRLDL MMKSGMFEEI AEFHRSKKAP
KEPLGIWKAI GVQEFDDYLK MYKWDNDMDK WDPMRKEAYE KAVRAIKENT FQLTKDQITK
INKLRNAGWD IKKVDATASF REAIRAAKEG EGVAEMQRKI WNKEVLEPCV KIVRSHLDQP
INYYYYYFYL LKRFLSLN
