ID   IPT_RHOFA               Reviewed;         255 AA.
AC   P46376;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Adenylate dimethylallyltransferase;
DE            EC=2.5.1.27;
DE   AltName: Full=Dimethylallyl transferase;
DE   AltName: Full=Isopentenyl transferase;
GN   Name=fas4; Synonyms=ipt;
OS   Rhodococcus fascians.
OG   Plasmid pFiD188.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1828;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D188;
RX   PubMed=8169198; DOI=10.1128/jb.176.9.2492-2501.1994;
RA   Crespi M., Vereecke D., Temmerman W., van Montagu M., Desomer J.;
RT   "The fas operon of Rhodococcus fascians encodes new genes required for
RT   efficient fasciation of host plants.";
RL   J. Bacteriol. 176:2492-2501(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D188;
RX   PubMed=1547783; DOI=10.1002/j.1460-2075.1992.tb05116.x;
RA   Crespi M., Messens E., Caplan A.B., van Montagu M., Desomer J.;
RT   "Fasciation induction by the phytopathogen Rhodococcus fascians depends
RT   upon a linear plasmid encoding a cytokinin synthase gene.";
RL   EMBO J. 11:795-804(1992).
CC   -!- FUNCTION: Transfers dimethylallyl groups to AMP as part of the
CC       biosynthesis of cytokinin phytohormones. {ECO:0000250}.
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   -!- INDUCTION: During the interaction with host plants.
CC   -!- SIMILARITY: Belongs to the isopentenyl transferase family.
CC       {ECO:0000305}.
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DR   EMBL; Z29635; CAA82744.1; -; Genomic_DNA.
DR   EMBL; X62428; CAA44294.1; -; Genomic_DNA.
DR   PIR; D55578; D55578.
DR   RefSeq; WP_015586134.1; NZ_NPFU01000019.1.
DR   RefSeq; YP_007878707.1; NC_021080.1.
DR   AlphaFoldDB; P46376; -.
DR   SMR; P46376; -.
DR   GeneID; 29801204; -.
DR   GO; GO:0009824; F:AMP dimethylallyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009691; P:cytokinin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR039657; Dimethylallyltransferase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002648; Tzs.
DR   PANTHER; PTHR11088; PTHR11088; 1.
DR   PANTHER; PTHR11088:SF28; PTHR11088:SF28; 1.
DR   PIRSF; PIRSF000507; IPT; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Cytokinin biosynthesis; Plasmid; Transferase.
FT   CHAIN           1..255
FT                   /note="Adenylate dimethylallyltransferase"
FT                   /id="PRO_0000216440"
SQ   SEQUENCE   255 AA;  28035 MW;  E524F0BE9FB65C9E CRC64;
     MKESTMAQTQ ARFDRVRWEP GVYAIVGATG IGKSAEASKL ALSHSAPIVV ADRIQCYSDL
     LVTSGRAFDA KVEGLNRVWL DNRTIHQGNF DPDEAFDRLI KVLTSYVDRG EAVVMEGGSI
     SLILRFAQTI SNLPFPAVVN VMPIPDRQHY FAQQCARARQ MLRGDSTGRN LLTELAEAWV
     LGDQHNFIAS VAGLDCVLDW CATHSVTPEE LANRDLTTEV LDELAASMGG RYVEHGVLQQ
     EIFLRTFGAP GVTAR