POK_THEKO
ID POK_THEKO Reviewed; 300 AA.
AC Q5JHF1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Pantoate kinase {ECO:0000255|HAMAP-Rule:MF_02223, ECO:0000303|PubMed:19666462};
DE Short=PoK {ECO:0000255|HAMAP-Rule:MF_02223, ECO:0000303|PubMed:19666462};
DE EC=2.7.1.169 {ECO:0000255|HAMAP-Rule:MF_02223, ECO:0000269|PubMed:19666462};
GN OrderedLocusNames=TK2141;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ROLE IN COA BIOSYNTHESIS, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=19666462; DOI=10.1074/jbc.m109.009696;
RA Yokooji Y., Tomita H., Atomi H., Imanaka T.;
RT "Pantoate kinase and phosphopantothenate synthetase, two novel enzymes
RT necessary for CoA biosynthesis in the Archaea.";
RL J. Biol. Chem. 284:28137-28145(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF SER-28; SER-104; HIS-131; GLU-134; ASP-143;
RP ARG-155 AND THR-186.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=22865846; DOI=10.1128/jb.06624-11;
RA Tomita H., Yokooji Y., Ishibashi T., Imanaka T., Atomi H.;
RT "Biochemical characterization of pantoate kinase, a novel enzyme necessary
RT for coenzyme A biosynthesis in the Archaea.";
RL J. Bacteriol. 194:5434-5443(2012).
CC -!- FUNCTION: Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in
CC the CoA biosynthesis pathway (PubMed:19666462, PubMed:22865846).
CC Displays broad nucleotide specificity and utilizes ATP, GTP, UTP, and
CC CTP with comparable catalytic efficiencies (PubMed:22865846).
CC {ECO:0000269|PubMed:19666462, ECO:0000269|PubMed:22865846}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + ATP = (R)-4-phosphopantoate + ADP + H(+);
CC Xref=Rhea:RHEA:28246, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61294, ChEBI:CHEBI:456216;
CC EC=2.7.1.169; Evidence={ECO:0000255|HAMAP-Rule:MF_02223,
CC ECO:0000269|PubMed:19666462, ECO:0000269|PubMed:22865846};
CC -!- ACTIVITY REGULATION: Moderately stimulated in the presence of potassium
CC cations. Inhibited by increasing concentrations of pantoate. Activity
CC is not affected by CoA/acetyl-CoA. {ECO:0000269|PubMed:22865846}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.47 mM for ATP {ECO:0000269|PubMed:19666462};
CC KM=0.45 mM for ATP {ECO:0000269|PubMed:22865846};
CC KM=0.43 mM for GTP {ECO:0000269|PubMed:22865846};
CC KM=0.17 mM for UTP {ECO:0000269|PubMed:22865846};
CC KM=0.34 mM for CTP {ECO:0000269|PubMed:22865846};
CC KM=1.2 mM for (R)-pantoate {ECO:0000269|PubMed:19666462};
CC KM=1.3 mM for (R)-pantothenate {ECO:0000269|PubMed:19666462};
CC Vmax=2870 nmol/min/mg enzyme toward (R)-pantoate
CC {ECO:0000269|PubMed:19666462};
CC Vmax=390 nmol/min/mg enzyme toward (R)-pantothenate
CC {ECO:0000269|PubMed:19666462};
CC Vmax=1.82 umol/min/mg enzyme toward ATP
CC {ECO:0000269|PubMed:22865846};
CC Vmax=0.58 umol/min/mg enzyme toward GTP
CC {ECO:0000269|PubMed:22865846};
CC Vmax=2.03 umol/min/mg enzyme toward UTP
CC {ECO:0000269|PubMed:22865846};
CC Vmax=0.87 umol/min/mg enzyme toward CTP
CC {ECO:0000269|PubMed:22865846};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:22865846};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:22865846};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02223, ECO:0000269|PubMed:19666462}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19666462}.
CC -!- DISRUPTION PHENOTYPE: Only viable in the presence of CoA or 4'-
CC phosphopantothenate. {ECO:0000269|PubMed:19666462}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. PoK subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02223, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP006878; BAD86330.1; -; Genomic_DNA.
DR RefSeq; WP_011251091.1; NC_006624.1.
DR PDB; 6JBC; X-ray; 2.70 A; A=1-300.
DR PDB; 6JBD; X-ray; 2.50 A; A=1-300.
DR PDBsum; 6JBC; -.
DR PDBsum; 6JBD; -.
DR AlphaFoldDB; Q5JHF1; -.
DR SMR; Q5JHF1; -.
DR STRING; 69014.TK2141; -.
DR EnsemblBacteria; BAD86330; BAD86330; TK2141.
DR GeneID; 3235456; -.
DR KEGG; tko:TK2141; -.
DR PATRIC; fig|69014.16.peg.2097; -.
DR eggNOG; arCOG04263; Archaea.
DR HOGENOM; CLU_081191_0_0_2; -.
DR InParanoid; Q5JHF1; -.
DR OMA; MLGETVF; -.
DR OrthoDB; 104702at2157; -.
DR PhylomeDB; Q5JHF1; -.
DR BioCyc; MetaCyc:MON-15970; -.
DR BRENDA; 2.7.1.169; 5246.
DR BRENDA; 2.7.1.33; 5246.
DR SABIO-RK; Q5JHF1; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_02223; Pantoate_kinase; 1.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR012043; PoK.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR42282; PTHR42282; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF016896; GHMP_arc_MJ0969; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..300
FT /note="Pantoate kinase"
FT /id="PRO_0000409259"
FT MUTAGEN 28
FT /note="S->A: Does not affect kinetics toward ATP but
FT decreases affinity for pantoate."
FT /evidence="ECO:0000269|PubMed:22865846"
FT MUTAGEN 104
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22865846"
FT MUTAGEN 131
FT /note="H->A: Does not affect kinetics toward ATP but
FT significantly decreases affinity for pantoate."
FT /evidence="ECO:0000269|PubMed:22865846"
FT MUTAGEN 134
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22865846"
FT MUTAGEN 143
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22865846"
FT MUTAGEN 155
FT /note="R->A: Decreases affinities for both ATP and
FT pantoate."
FT /evidence="ECO:0000269|PubMed:22865846"
FT MUTAGEN 186
FT /note="T->A: Displays a defect in dimer assembly. Does not
FT affect Km for ATP but the affinity for pantoate decreases
FT dramatically."
FT /evidence="ECO:0000269|PubMed:22865846"
FT STRAND 2..18
FT /evidence="ECO:0007829|PDB:6JBD"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 27..47
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:6JBD"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:6JBD"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6JBD"
FT HELIX 103..119
FT /evidence="ECO:0007829|PDB:6JBD"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:6JBD"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:6JBD"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:6JBD"
FT HELIX 193..211
FT /evidence="ECO:0007829|PDB:6JBD"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:6JBD"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:6JBD"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:6JBD"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:6JBD"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:6JBD"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:6JBD"
SQ SEQUENCE 300 AA; 32750 MW; 88A413C58F545D16 CRC64;
MLIRAFIPAH ITAFFVPVFH EEPLKAGSLG AGVNLSKGTN VFASIETGTL ERHIHVAFNG
EPVKREEAEI TYYVAEKLVP KDFLGEVEVW QYFDFPNGYG FGNSAGGALG TALALSYAFG
GTWLRAAQLA HEAEVKHKGG LGDVIGQLAG GIEVRIKPGG PGIGVTDNLF FEDYKVLVVP
LGRLSTREVL DGDVVKAIEV EGRKALEELL KEPKPERMMV LARNFAEKTG LLPGELSEIA
RELDKVLKNP SSMIMLGKGL FALVRDEEAE KAKQLLSDMN LPYDIAEIYT ERPKVGRWVG
