IPT5_ARATH
ID IPT5_ARATH Reviewed; 330 AA.
AC Q94ID2; Q94IC9;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Adenylate isopentenyltransferase 5, chloroplastic;
DE Short=AtIPT5;
DE EC=2.5.1.112;
DE AltName: Full=Adenylate dimethylallyltransferase 5;
DE AltName: Full=Cytokinin synthase 5;
DE Flags: Precursor;
GN Name=IPT5; OrderedLocusNames=At5g19040; ORFNames=T16G12.80;
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], CATALYTIC 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=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 [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, DEVELOPMENTAL STAGE, 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 [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
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 [8]
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 [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 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 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:14726522}.
CC -!- TISSUE SPECIFICITY: Expressed in root primordia, columella root caps,
CC upper part of young inflorescences, and fruit abscission zones.
CC {ECO:0000269|PubMed:14675438, ECO:0000269|PubMed:15356331}.
CC -!- DEVELOPMENTAL STAGE: Expressed in roots soon after germination, but
CC decreases 7 days after germination. {ECO:0000269|PubMed:14675438}.
CC -!- INDUCTION: Down-regulated by cytokinins and up-regulated by auxin. Not
CC induced by nitrate. {ECO:0000269|PubMed:14675438,
CC ECO:0000269|PubMed:15356331}.
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; AB062608; BAB59041.1; -; mRNA.
DR EMBL; AB061403; BAB59032.1; -; mRNA.
DR EMBL; AC068809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92645.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70556.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70557.1; -; Genomic_DNA.
DR RefSeq; NP_001318596.1; NM_001343584.1.
DR RefSeq; NP_001332154.1; NM_001343585.1.
DR RefSeq; NP_197405.1; NM_121909.2.
DR AlphaFoldDB; Q94ID2; -.
DR SMR; Q94ID2; -.
DR STRING; 3702.AT5G19040.1; -.
DR PaxDb; Q94ID2; -.
DR PRIDE; Q94ID2; -.
DR EnsemblPlants; AT5G19040.1; AT5G19040.1; AT5G19040.
DR EnsemblPlants; AT5G19040.2; AT5G19040.2; AT5G19040.
DR EnsemblPlants; AT5G19040.3; AT5G19040.3; AT5G19040.
DR GeneID; 832023; -.
DR Gramene; AT5G19040.1; AT5G19040.1; AT5G19040.
DR Gramene; AT5G19040.2; AT5G19040.2; AT5G19040.
DR Gramene; AT5G19040.3; AT5G19040.3; AT5G19040.
DR KEGG; ath:AT5G19040; -.
DR Araport; AT5G19040; -.
DR TAIR; locus:2179629; AT5G19040.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_4_1_1; -.
DR InParanoid; Q94ID2; -.
DR OMA; NMHRVDA; -.
DR OrthoDB; 1003231at2759; -.
DR BioCyc; MetaCyc:AT5G19040-MON; -.
DR BRENDA; 2.5.1.112; 399.
DR PRO; PR:Q94ID2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94ID2; baseline and differential.
DR Genevisible; Q94ID2; 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; 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: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; Chloroplast; Cytokinin biosynthesis; Nucleotide-binding;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..330
FT /note="Adenylate isopentenyltransferase 5, chloroplastic"
FT /id="PRO_0000391073"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 177
FT /note="D -> E (in Ref. 2; BAB59032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 37395 MW; 145E0000E226CD03 CRC64;
MKPCMTALRQ VIQPLSLNFQ GNMVDVPFFR RKDKVVFVMG ATGTGKSRLA IDLATRFPAE
IVNSDKIQVY KGLDIVTNKV TPEESLGVPH HLLGTVHDTY EDFTAEDFQR EAIRAVESIV
QRDRVPIIAG GSNSYIEALV NDCVDFRLRY NCCFLWVDVS RPVLHSFVSE RVDKMVDMGL
VDEVRRIFDP SSSDYSAGIR RAIGVPELDE FLRSEMRNYP AETTERLLET AIEKIKENTC
LLACRQLQKI QRLYKQWKWN MHRVDATEVF LRRGEEADEA WDNSVAHPSA LAVEKFLSYS
DDHHLEGANI LLPEISAVPP LPAAVAAISR
