IPK_METTH
ID IPK_METTH Reviewed; 266 AA.
AC O26153;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Isopentenyl phosphate kinase;
DE Short=IPK;
DE EC=2.7.4.26;
GN OrderedLocusNames=MTH_47;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
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 (2.15 ANGSTROMS) IN COMPLEX WITH ADP, 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
CC dimethylallyl phosphate (DMAP) and isopentenyl thiolophosphate (ISP).
CC Has low activity with 1-butyl phosphate (BP) and 3-buten-1-yl phosphate
CC (BEP). Has no 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=12.7 uM for isopentenyl phosphate {ECO:0000269|PubMed:19928876};
CC KM=13.4 uM for ATP {ECO:0000269|PubMed:19928876};
CC pH dependence:
CC Optimum pH is 6.8-9.7. {ECO:0000269|PubMed:19928876};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius, but the enzyme is not
CC stable above 50 degrees Celsius. {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; AE000666; AAB84554.1; -; Genomic_DNA.
DR PIR; E69161; E69161.
DR RefSeq; WP_010875687.1; NC_000916.1.
DR PDB; 3LL9; X-ray; 2.15 A; A/B=1-266.
DR PDBsum; 3LL9; -.
DR AlphaFoldDB; O26153; -.
DR SMR; O26153; -.
DR STRING; 187420.MTH_47; -.
DR EnsemblBacteria; AAB84554; AAB84554; MTH_47.
DR GeneID; 1470009; -.
DR KEGG; mth:MTH_47; -.
DR PATRIC; fig|187420.15.peg.45; -.
DR HOGENOM; CLU_070213_0_0_2; -.
DR OMA; HHNASEH; -.
DR BRENDA; 2.7.4.26; 3256.
DR EvolutionaryTrace; O26153; -.
DR Proteomes; UP000005223; 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..266
FT /note="Isopentenyl phosphate kinase"
FT /id="PRO_0000424201"
FT BINDING 5..9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 183..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT SITE 14
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:3LL9"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 67..97
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3LL9"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3LL9"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:3LL9"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:3LL9"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3LL9"
SQ SEQUENCE 266 AA; 29084 MW; 848778BE1857CC13 CRC64;
MIILKLGGSV ITRKDSEEPA IDRDNLERIA SEIGNASPSS LMIVHGAGSF GHPFAGEYRI
GSEIENEEDL RRRRFGFALT QNWVKKLNSH VCDALLAEGI PAVSMQPSAF IRAHAGRISH
ADISLIRSYL EEGMVPVVYG DVVLDSDRRL KFSVISGDQL INHFSLRLMP ERVILGTDVD
GVYTRNPKKH PDARLLDVIG SLDDLESLDG TLNTDVTGGM VGKIRELLLL AEKGVESEII
NAAVPGNIER ALLGEEVRGT RITGKH
