IPK_HALVD
ID IPK_HALVD Reviewed; 248 AA.
AC D4GWT7;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Isopentenyl phosphate kinase;
DE Short=IPK;
DE EC=2.7.4.26;
GN OrderedLocusNames=HVO_2762; ORFNames=C498_09099;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND
RP PATHWAY.
RC STRAIN=DS2 / DS70;
RX PubMed=24375100; DOI=10.1128/jb.01230-13;
RA Vannice J.C., Skaff D.A., Keightley A., Addo J.K., Wyckoff G.J.,
RA Miziorko H.M.;
RT "Identification in Haloferax volcanii of phosphomevalonate decarboxylase
RT and isopentenyl phosphate kinase as catalysts of the terminal enzyme
RT reactions in an archaeal alternate mevalonate pathway.";
RL J. Bacteriol. 196:1055-1063(2014).
CC -!- FUNCTION: Catalyzes the phosphorylation of isopentenyl phosphate (IP)
CC to isopentenyl diphosphate (IPP). Functions in an alternate mevalonate
CC (MVA) pathway leading to IPP, a key precursor for the biosynthesis of
CC isoprenoid compounds such as archaeal membrane lipids.
CC {ECO:0000269|PubMed:24375100}.
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:24375100};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=77 uM for isopentenyl phosphate {ECO:0000269|PubMed:24375100};
CC KM=290 uM for ATP {ECO:0000269|PubMed:24375100};
CC Vmax=37 umol/min/mg enzyme {ECO:0000269|PubMed:24375100};
CC Note=kcat is 16.3 sec(-1).;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the isopentenyl phosphate kinase family.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE04091.1; -; Genomic_DNA.
DR EMBL; AOHU01000047; ELY32354.1; -; Genomic_DNA.
DR RefSeq; WP_004043009.1; NZ_AOHU01000047.1.
DR AlphaFoldDB; D4GWT7; -.
DR SMR; D4GWT7; -.
DR STRING; 309800.C498_09099; -.
DR EnsemblBacteria; ADE04091; ADE04091; HVO_2762.
DR EnsemblBacteria; ELY32354; ELY32354; C498_09099.
DR GeneID; 8924706; -.
DR KEGG; hvo:HVO_2762; -.
DR PATRIC; fig|309800.29.peg.1783; -.
DR eggNOG; arCOG00860; Archaea.
DR HOGENOM; CLU_070213_0_0_2; -.
DR OMA; HHNASEH; -.
DR OrthoDB; 96284at2157; -.
DR BioCyc; MetaCyc:MON-21129; -.
DR BRENDA; 2.7.4.26; 2561.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
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 ATP-binding; Isoprene biosynthesis; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..248
FT /note="Isopentenyl phosphate kinase"
FT /id="PRO_0000429254"
FT BINDING 7..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 16
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 248 AA; 24647 MW; 157DD8C84A219B8F CRC64;
MSLVVLKLGG SVVTDKDEPE TVDEAGLAAA ADAVAPLAES RRVVVVHGGG SFGHHHAAEH
GVSSESGSHD ARGVRAIHDA MKRLNDAVLD ALEERGVAAL PVHPLSAGAR EADGSLSLPL
AATETMLDEG FVPVLHGDVI SHAGKGATIV SGDDLVVSLA SGLGADRVGL CSTVPGVLDA
DGDVIPEITA FADAADALGG SDSTDVTGGM AAKVRKLLAL GAPAHVFGPE GLSAFVAGES
PGTVIRGE
