ID   IPT_AGRVS               Reviewed;         236 AA.
AC   Q04590; B9K457;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Adenylate dimethylallyltransferase;
DE            EC=2.5.1.27;
DE   AltName: Full=Dimethylallyl transferase;
DE   AltName: Full=Isopentenyl transferase;
GN   Name=ipt; OrderedLocusNames=Avi_8294;
OS   Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain
OS   S4)).
OG   Plasmid pTiS4.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=311402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1465104; DOI=10.1007/bf00279373;
RA   Canaday J., Gerard J.-C., Crouzet P., Otten L.;
RT   "Organization and functional analysis of three T-DNAs from the vitopine Ti
RT   plasmid pTiS4.";
RL   Mol. Gen. Genet. 235:292-303(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 / ATCC BAA-846;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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   -!- SIMILARITY: Belongs to the isopentenyl transferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M91610; AAA98150.1; -; Genomic_DNA.
DR   EMBL; CP000637; ACM39711.1; -; Genomic_DNA.
DR   PIR; S30106; S30106.
DR   RefSeq; WP_012649069.1; NC_011982.1.
DR   AlphaFoldDB; Q04590; -.
DR   SMR; Q04590; -.
DR   EnsemblBacteria; ACM39711; ACM39711; Avi_8294.
DR   KEGG; avi:Avi_8294; -.
DR   HOGENOM; CLU_1115409_0_0_5; -.
DR   OMA; RIAQEYW; -.
DR   OrthoDB; 1502215at2; -.
DR   Proteomes; UP000001596; Plasmid pTiS4.
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   3: Inferred from homology;
KW   Crown gall tumor; Cytokinin biosynthesis; Plasmid; Reference proteome;
KW   Transferase.
FT   CHAIN           1..236
FT                   /note="Adenylate dimethylallyltransferase"
FT                   /id="PRO_0000216434"
SQ   SEQUENCE   236 AA;  25841 MW;  91ECCE9A17F2D1DF CRC64;
     MEAHLIFGPT STGKTSVAIA LAKRTGFPVI VLDRIQCYSQ LSVGGGRPSA AEFQGTRRIY
     LIEGSLDEGV ISAERAHECL VAAVEAHKPE GGVILEGGSI SLFKRMAQSS YWNCGFTWHV
     TRLHLGGEEI FLAAAKKRIN QMMQPDEQGN SFLGELVSVW KTTALRATLE GICGYRYAIE
     FAGKQGLEMD ALTSLNRRQL EQLVHGMAHE YLCYARQQEQ ELPLPSLAGG EGPPFQ