DPCKG_THEKO
ID DPCKG_THEKO Reviewed; 177 AA.
AC Q5JIY7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=GTP-dependent dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00590, ECO:0000303|PubMed:31337720};
DE EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_00590, ECO:0000269|PubMed:31337720};
DE AltName: Full=Dephospho-coenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00590, ECO:0000303|PubMed:31337720};
DE Short=DPCK {ECO:0000255|HAMAP-Rule:MF_00590, ECO:0000303|PubMed:31337720};
GN OrderedLocusNames=TK1697 {ECO:0000312|EMBL:BAD85886.1};
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, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-48; ASP-67 AND
RP ASP-125.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=31337720; DOI=10.1128/mbio.01146-19;
RA Shimosaka T., Makarova K.S., Koonin E.V., Atomi H.;
RT "Identification of dephospho-coenzyme A (dephospho-CoA) kinase in
RT Thermococcus kodakarensis and elucidation of the entire CoA biosynthesis
RT pathway in archaea.";
RL MBio 10:E01146-E01146(2019).
CC -!- FUNCTION: Catalyzes the GTP-dependent phosphorylation of the 3'-
CC hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA). Can
CC also use UTP, with lower efficiency and has weak activity with ATP, but
CC shows a strong preference for GTP as the phosphate donor.
CC {ECO:0000269|PubMed:31337720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + GTP = CoA + GDP + H(+);
CC Xref=Rhea:RHEA:61156, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00590,
CC ECO:0000269|PubMed:31337720};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for dephospho-CoA {ECO:0000269|PubMed:31337720};
CC KM=0.26 mM for GTP {ECO:0000269|PubMed:31337720};
CC Vmax=17.0 umol/min/mg enzyme toward dephospho-CoA
CC {ECO:0000269|PubMed:31337720};
CC Vmax=20.4 umol/min/mg enzyme toward GTP
CC {ECO:0000269|PubMed:31337720};
CC Note=kcat is 5.57 sec(-1). {ECO:0000269|PubMed:31337720};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:31337720};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:31337720};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00590, ECO:0000269|PubMed:31337720}.
CC -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:31337720}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene results in CoA auxotrophy.
CC {ECO:0000269|PubMed:31337720}.
CC -!- SIMILARITY: Belongs to the GTP-dependent DPCK family.
CC {ECO:0000255|HAMAP-Rule:MF_00590, ECO:0000305}.
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DR EMBL; AP006878; BAD85886.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5JIY7; -.
DR STRING; 69014.TK1697; -.
DR EnsemblBacteria; BAD85886; BAD85886; TK1697.
DR KEGG; tko:TK1697; -.
DR PATRIC; fig|69014.16.peg.1655; -.
DR eggNOG; arCOG04076; Archaea.
DR HOGENOM; CLU_120795_1_0_2; -.
DR InParanoid; Q5JIY7; -.
DR OMA; AIYDHKT; -.
DR PhylomeDB; Q5JIY7; -.
DR BioCyc; MetaCyc:MON-21893; -.
DR BRENDA; 2.7.1.24; 5246.
DR BRENDA; 2.7.1.B30; 5246.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000536; Chromosome.
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_00590; Dephospho_CoA_kinase_GTP_dep; 1.
DR InterPro; IPR007164; GTP-dep_dephospho-CoA_kin.
DR PANTHER; PTHR40732; PTHR40732; 1.
DR Pfam; PF04019; DUF359; 1.
DR PIRSF; PIRSF006533; UCP006533; 1.
PE 1: Evidence at protein level;
KW Coenzyme A biosynthesis; Kinase; Reference proteome; Transferase.
FT CHAIN 1..177
FT /note="GTP-dependent dephospho-CoA kinase"
FT /id="PRO_0000137617"
FT MUTAGEN 48
FT /note="D->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:31337720"
FT MUTAGEN 67
FT /note="D->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:31337720"
FT MUTAGEN 125
FT /note="D->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:31337720"
SQ SEQUENCE 177 AA; 19657 MW; E124928443928378 CRC64;
MKMFFRLTRE LRDELKRPLG ELVRGPIPEP YLKVRGELEK HPVVTVGDVV TENVLKIGVK
PIIALYDLKT KRKEYSPEIE DTAVFLTVTN PPGTITKALL DTVRKAFGLA ERGRNVHILV
SGEEDLAAIP AVLYAPLGTL VLYGQPDEGV VLIKVTPECK RRCAKILASM EVVRDGD
