IPT_HUMLU
ID IPT_HUMLU Reviewed; 329 AA.
AC Q5GHF7;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Adenylate isopentenyltransferase {ECO:0000303|PubMed:15381407, ECO:0000303|PubMed:20007608};
DE Short=HlAIPT {ECO:0000303|PubMed:20007608};
DE EC=2.5.1.112 {ECO:0000269|PubMed:15381407};
DE EC=2.5.1.27 {ECO:0000269|PubMed:15381407};
DE AltName: Full=Adenylate dimethylallyltransferase {ECO:0000303|PubMed:15381407};
DE AltName: Full=Cytokinin synthase {ECO:0000303|PubMed:15381407};
GN Name=AIPT {ECO:0000303|PubMed:15381407, ECO:0000303|PubMed:20007608};
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ASP-62, FUNCTION, TISSUE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RX PubMed=15381407; DOI=10.1016/j.phytochem.2004.08.006;
RA Sakano Y., Okada Y., Matsunaga A., Suwama T., Kaneko T., Ito K.,
RA Noguchi H., Abe I.;
RT "Molecular cloning, expression, and characterization of adenylate
RT isopentenyltransferase from hop (Humulus lupulus L.).";
RL Phytochemistry 65:2439-2446(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) IN COMPLEX WITH ATP.
RX PubMed=20007608; DOI=10.1093/nar/gkp1093;
RA Chu H.M., Ko T.P., Wang A.H.;
RT "Crystal structure and substrate specificity of plant adenylate
RT isopentenyltransferase from Humulus lupulus: distinctive binding affinity
RT for purine and pyrimidine nucleotides.";
RL Nucleic Acids Res. 38:1738-1748(2010).
CC -!- FUNCTION: Involved in cytokinin biosynthesis. Catalyzes the transfer of
CC an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP, ADP
CC and AMP. GMP, IMP, CMP or UMP are not used as substrates.
CC {ECO:0000269|PubMed:15381407}.
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 Evidence={ECO:0000269|PubMed:15381407};
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:15381407};
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:15381407};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15381407};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=759 uM for AMP {ECO:0000269|PubMed:15381407};
CC KM=19.3 uM for ADP {ECO:0000269|PubMed:15381407};
CC KM=16.2 uM for ATP {ECO:0000269|PubMed:15381407};
CC KM=19.5 uM for DMAPP {ECO:0000269|PubMed:15381407};
CC pH dependence:
CC Optimum pH is 6.0-9.0. {ECO:0000269|PubMed:15381407};
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and cones.
CC {ECO:0000269|PubMed:15381407}.
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR EMBL; AY533024; AAS94327.1; -; Genomic_DNA.
DR PDB; 3A8T; X-ray; 2.37 A; A=1-329.
DR PDBsum; 3A8T; -.
DR AlphaFoldDB; Q5GHF7; -.
DR SMR; Q5GHF7; -.
DR KEGG; ag:AAS94327; -.
DR BRENDA; 2.5.1.112; 2716.
DR BRENDA; 2.5.1.27; 2716.
DR BRENDA; 2.5.1.75; 2716.
DR SABIO-RK; Q5GHF7; -.
DR EvolutionaryTrace; Q5GHF7; -.
DR GO; GO:0009824; F:AMP dimethylallyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034265; P:isopentenyl adenine biosynthetic process; IC:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR039657; Dimethylallyltransferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11088; PTHR11088; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytokinin biosynthesis; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..329
FT /note="Adenylate isopentenyltransferase"
FT /id="PRO_0000391078"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20007608,
FT ECO:0007744|PDB:3A8T"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20007608,
FT ECO:0007744|PDB:3A8T"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20007608,
FT ECO:0007744|PDB:3A8T"
FT BINDING 129..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20007608,
FT ECO:0007744|PDB:3A8T"
FT BINDING 220..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20007608,
FT ECO:0007744|PDB:3A8T"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20007608,
FT ECO:0007744|PDB:3A8T"
FT MUTAGEN 62
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15381407"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:3A8T"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3A8T"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3A8T"
FT TURN 71..75
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3A8T"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:3A8T"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:3A8T"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3A8T"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 174..191
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 247..279
FT /evidence="ECO:0007829|PDB:3A8T"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:3A8T"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:3A8T"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:3A8T"
SQ SEQUENCE 329 AA; 36605 MW; 6C97C1D0F7DBD720 CRC64;
MDYASVAMAA APTTTTTTNV SLRRQRHRKE KLLVLMGATG TGKSRLSIDL AAHFPLEVIN
SDKMQVYKGL DITTNKISVP DRGGVPHHLL GEVDPARGEL TPADFRSLAG KAVSEITGRR
KLPVLVGGSN SFIHALLVDR FDSSGPGVFE EGSHSVVSSE LRYDCCFLWV DVSVKVLTDY
LAKRVDDMLE LGMFDELAEF YSPEDEDHDE DSATRTGLRK AIGVPEFDRY FEKFRPGDVE
GEDPGRDRVR RGAFEEAVRA IKENTCHLAK RQIGKILRLK GAGWDLRRLD ATESFRAAMT
SDSGEKCTEI WEKQVLEPSV KIVSRFLDE
