IPTZ_AGRFC
ID IPTZ_AGRFC Reviewed; 243 AA.
AC P58758;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Adenylate dimethylallyltransferase;
DE EC=2.5.1.27;
DE AltName: Full=Dimethylallyl transferase;
DE AltName: Full=Isopentenyl transferase;
DE AltName: Full=Trans-zeatin producing protein;
GN Name=tzs; OrderedLocusNames=Atu6164; ORFNames=AGR_pTi_290;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OG Plasmid pTiC58.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Beaty J.S., Powell G.K., Lica L., Regier D.A., McDonald E.M.S.,
RA Hommes N.G., Morris R.O.;
RT "Tzs, a nopaline Ti plasmid gene from Agrobacterium tumefaciens associated
RT with trans-zeatin biosynthesis.";
RL Mol. Gen. Genet. 203:274-280(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2194232; DOI=10.1016/0147-619x(90)90028-b;
RA Rogowsky P.M., Powell B.S., Shirasu K., Lin T.-S., Morel P., Zyprian E.M.,
RA Steck T.R., Kado C.I.;
RT "Molecular characterization of the vir regulon of Agrobacterium
RT tumefaciens: complete nucleotide sequence and gene organization of the
RT 28.63-kbp regulon cloned as a single unit.";
RL Plasmid 23:85-106(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX DOI=10.1071/PP9930621;
RA Morris R.O., Blevins D.G., Dietrich J.T., Durley R.C., Gelvin S.B.,
RA Gray J., Hommes N.G., Kaminek M., Mathews L.J., Meilan R.;
RT "Cytokinins in plant pathogenic bacteria and developing cereal grains.";
RL Aust. J. Plant Physiol. 20:621-637(1993).
CC -!- FUNCTION: Transfers dimethylallyl groups to AMP as part of the
CC biosynthesis of cytokinin phytohormones. {ECO:0000269|Ref.5}.
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; Evidence={ECO:0000269|Ref.5};
CC -!- INTERACTION:
CC P58758; P17795: virB5; NbExp=4; IntAct=EBI-6402098, EBI-6400510;
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DR EMBL; X03933; CAA27572.1; -; Genomic_DNA.
DR EMBL; J03320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE007871; AAK91123.2; -; Genomic_DNA.
DR PIR; AB3248; AB3248.
DR PIR; S03122; S03122.
DR RefSeq; NP_396682.2; NC_003065.3.
DR RefSeq; WP_010974913.1; NC_003065.3.
DR PDB; 2ZE5; X-ray; 2.31 A; A=1-243.
DR PDB; 2ZE6; X-ray; 2.10 A; A=1-243.
DR PDB; 2ZE7; X-ray; 2.10 A; A=1-243.
DR PDB; 2ZE8; X-ray; 2.80 A; A/B/C/D=1-243.
DR PDBsum; 2ZE5; -.
DR PDBsum; 2ZE6; -.
DR PDBsum; 2ZE7; -.
DR PDBsum; 2ZE8; -.
DR AlphaFoldDB; P58758; -.
DR SMR; P58758; -.
DR IntAct; P58758; 1.
DR DrugBank; DB02270; Dimethylallyl S-Thiolodiphosphate.
DR EnsemblBacteria; AAK91123; AAK91123; Atu6164.
DR KEGG; atu:Atu6164; -.
DR HOGENOM; CLU_1115409_0_0_5; -.
DR OMA; RIAQEYW; -.
DR BioCyc; AGRO:ATU6164-MON; -.
DR BRENDA; 2.5.1.27; 200.
DR EvolutionaryTrace; P58758; -.
DR Proteomes; UP000000813; Plasmid Ti.
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 1: Evidence at protein level;
KW 3D-structure; Crown gall tumor; Cytokinin biosynthesis; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..243
FT /note="Adenylate dimethylallyltransferase"
FT /id="PRO_0000216441"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2ZE6"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2ZE5"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:2ZE6"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2ZE6"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:2ZE6"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2ZE8"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:2ZE6"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:2ZE6"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:2ZE6"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:2ZE6"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:2ZE6"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:2ZE6"
FT HELIX 199..221
FT /evidence="ECO:0007829|PDB:2ZE6"
SQ SEQUENCE 243 AA; 27591 MW; 59D3743BA14B6AA5 CRC64;
MLLHLIYGPT CSGKTDMAIQ IAQETGWPVV ALDRVQCCPQ IATGSGRPLE SELQSTRRIY
LDSRPLTEGI LDAESAHRRL IFEVDWRKSE EGLILEGGSI SLLNCMAKSP FWRSGFQWHV
KRLRLGDSDA FLTRAKQRVA EMFAIREDRP SLLEELAELW NYPAARPILE DIDGYRCAIR
FARKHDLAIS QLPNIDAGRH VELIEAIANE YLEHALSQER DFPQWPEDGA GQPVCPVTLT
RIR
