IPK_THEAC
ID IPK_THEAC Reviewed; 245 AA.
AC Q9HLX1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Isopentenyl phosphate kinase;
DE Short=IPK;
DE EC=2.7.4.26;
GN OrderedLocusNames=Ta0103;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=19928876; DOI=10.1021/bi9017957;
RA Chen M., Poulter C.D.;
RT "Characterization of thermophilic archaeal isopentenyl phosphate kinases.";
RL Biochemistry 49:207-217(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEXES WITH ISOPENTENYL
RP PHOSPHATE AND ATP, AND SUBUNIT.
RX PubMed=20402538; DOI=10.1021/cb100032g;
RA Mabanglo M.F., Schubert H.L., Chen M., Hill C.P., Poulter C.D.;
RT "X-ray structures of isopentenyl phosphate kinase.";
RL ACS Chem. Biol. 5:517-527(2010).
CC -!- FUNCTION: Catalyzes the formation of isopentenyl diphosphate (IPP), the
CC building block of all isoprenoids. Has lower activity with isopentenyl
CC thiolophosphate (ISP). Has low activity with dimethylallyl phosphate
CC (DMAP), 1-butyl phosphate (BP) and 3-buten-1-yl phosphate (BEP). Has no
CC significant activity with geranyl phosphate (in vitro).
CC {ECO:0000269|PubMed:19928876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate;
CC Xref=Rhea:RHEA:33963, ChEBI:CHEBI:30616, ChEBI:CHEBI:65078,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=2.7.4.26;
CC Evidence={ECO:0000269|PubMed:19928876};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for isopentenyl phosphate {ECO:0000269|PubMed:19928876};
CC KM=6.0 uM for ATP {ECO:0000269|PubMed:19928876};
CC pH dependence:
CC Optimum pH is 6.5-8.5. {ECO:0000269|PubMed:19928876};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:19928876};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19928876,
CC ECO:0000269|PubMed:20402538}.
CC -!- SIMILARITY: Belongs to the isopentenyl phosphate kinase family.
CC {ECO:0000305}.
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DR EMBL; AL445063; CAC11251.1; -; Genomic_DNA.
DR RefSeq; WP_010900530.1; NC_002578.1.
DR PDB; 3LKK; X-ray; 2.00 A; A/B=1-245.
DR PDB; 3LL5; X-ray; 1.99 A; A/B/C/D=1-245.
DR PDBsum; 3LKK; -.
DR PDBsum; 3LL5; -.
DR AlphaFoldDB; Q9HLX1; -.
DR SMR; Q9HLX1; -.
DR STRING; 273075.Ta0103; -.
DR EnsemblBacteria; CAC11251; CAC11251; CAC11251.
DR GeneID; 1455758; -.
DR KEGG; tac:Ta0103; -.
DR eggNOG; arCOG00860; Archaea.
DR HOGENOM; CLU_070213_0_0_2; -.
DR OMA; HHNASEH; -.
DR OrthoDB; 96284at2157; -.
DR BioCyc; MetaCyc:MON-18737; -.
DR BRENDA; 2.7.4.26; 6324.
DR EvolutionaryTrace; Q9HLX1; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0102043; F:isopentenyl phosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04241; AAK_FomA-like; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR024192; Fosfomycin_R_FomA-type.
DR PANTHER; PTHR43654:SF1; PTHR43654:SF1; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF016496; Kin_FomA; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Isoprene biosynthesis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..245
FT /note="Isopentenyl phosphate kinase"
FT /id="PRO_0000424200"
FT BINDING 5..9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 45
FT /ligand="substrate"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 50
FT /ligand="substrate"
FT BINDING 143
FT /ligand="substrate"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 169..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT SITE 14
FT /note="Transition state stabilizer"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 64..90
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3LL5"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:3LL5"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:3LL5"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3LL5"
SQ SEQUENCE 245 AA; 27050 MW; 1C8F2140B89CDE48 CRC64;
MMILKIGGSV ITDKSAYRTA RTYAIRSIVK VLSGIEDLVC VVHGGGSFGH IKAMEFGLPG
PKNPRSSIGY SIVHRDMENL DLMVIDAMIE MGMRPISVPI SALRYDGRFD YTPLIRYIDA
GFVPVSYGDV YIKDEHSYGI YSGDDIMADM AELLKPDVAV FLTDVDGIYS KDPKRNPDAV
LLRDIDTNIT FDRVQNDVTG GIGKKFESMV KMKSSVKNGV YLINGNHPER IGDIGKESFI
GTVIR
