R1PK_THEKO
ID R1PK_THEKO Reviewed; 294 AA.
AC Q5JDG9;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=ADP-dependent ribose-1-phosphate kinase {ECO:0000303|PubMed:25822915};
DE Short=ADP-R1P kinase {ECO:0000303|PubMed:25822915};
DE EC=2.7.1.212 {ECO:0000269|PubMed:25822915};
DE AltName: Full=ADP:alpha-D-ribose-1-phosphate 5-phosphotransferase {ECO:0000305};
DE AltName: Full=Alpha-D-ribose-1-phosphate 5-kinase (ADP) {ECO:0000305};
GN OrderedLocusNames=TK2029 {ECO:0000312|EMBL:BAD86218.1};
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, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=25822915; DOI=10.1038/nchembio.1786;
RA Aono R., Sato T., Imanaka T., Atomi H.;
RT "A pentose bisphosphate pathway for nucleoside degradation in Archaea.";
RL Nat. Chem. Biol. 11:355-360(2015).
CC -!- FUNCTION: Involved in nucleoside degradation. Phosphorylates ribose 1-
CC phosphate (R1P) to ribose 1,5-bisphosphate. Can also act on deoxyribose
CC 1-phosphate (dR1P), but is most active with R1P. ADP is the most
CC preferred phosphate donor, followed by GDP and UDP.
CC {ECO:0000269|PubMed:25822915}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + alpha-D-ribose 1-phosphate = alpha-D-ribose 1,5-
CC bisphosphate + AMP + H(+); Xref=Rhea:RHEA:49416, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57720, ChEBI:CHEBI:68688, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; EC=2.7.1.212;
CC Evidence={ECO:0000269|PubMed:25822915};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25822915};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:25822915};
CC Note=Can use Mg(2+) and Ca(2+) with equal efficiency in vitro, and to a
CC lesser extent, Co(2+). {ECO:0000269|PubMed:25822915};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.53 mM for ribose 1-phosphate (in the presence of Mg(2+))
CC {ECO:0000269|PubMed:25822915};
CC KM=12 mM for deoxyribose 1-phosphate (in the presence of Mg(2+))
CC {ECO:0000269|PubMed:25822915};
CC KM=7.3 mM for ADP (in the presence of Mg(2+))
CC {ECO:0000269|PubMed:25822915};
CC KM=19 mM for GDP (in the presence of Mg(2+))
CC {ECO:0000269|PubMed:25822915};
CC Vmax=912 umol/min/mg enzyme with ribose 1-phosphate as substrate (in
CC the presence of Mg(2+)) {ECO:0000269|PubMed:25822915};
CC Vmax=137 umol/min/mg enzyme with deoxyribose 1-phosphate as substrate
CC (in the presence of Mg(2+)) {ECO:0000269|PubMed:25822915};
CC Vmax=1150 umol/min/mg enzyme toward ADP (in the presence of Mg(2+))
CC {ECO:0000269|PubMed:25822915};
CC Vmax=355 umol/min/mg enzyme toward GDP (in the presence of Mg(2+))
CC {ECO:0000269|PubMed:25822915};
CC Note=kcat is 485 sec(-1) with ribose 1-phosphate as substrate. kcat
CC is 73 sec(-1) with deoxyribose 1-phosphate as substrate. kcat is 612
CC sec(-1) with ADP as substrate. kcat is 189 sec(-1) with GDP as
CC substrate. {ECO:0000269|PubMed:25822915};
CC pH dependence:
CC High levels of activity within a broad pH range of 5.0-8.0.
CC {ECO:0000269|PubMed:25822915};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:25822915};
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AP006878; BAD86218.1; -; Genomic_DNA.
DR RefSeq; WP_011250979.1; NC_006624.1.
DR AlphaFoldDB; Q5JDG9; -.
DR SMR; Q5JDG9; -.
DR STRING; 69014.TK2029; -.
DR EnsemblBacteria; BAD86218; BAD86218; TK2029.
DR GeneID; 3235391; -.
DR KEGG; tko:TK2029; -.
DR PATRIC; fig|69014.16.peg.1983; -.
DR eggNOG; arCOG00014; Archaea.
DR HOGENOM; CLU_027634_6_0_2; -.
DR InParanoid; Q5JDG9; -.
DR OMA; TFCGYFA; -.
DR OrthoDB; 98664at2157; -.
DR PhylomeDB; Q5JDG9; -.
DR BioCyc; MetaCyc:MON-19660; -.
DR BRENDA; 2.7.1.212; 5246.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR002139; Ribo/fructo_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00990; RIBOKINASE.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Kinase; Magnesium; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..294
FT /note="ADP-dependent ribose-1-phosphate kinase"
FT /id="PRO_0000441669"
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 200..205
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
SQ SEQUENCE 294 AA; 31915 MW; 49323269CB1C1BA1 CRC64;
MKLDVIGIGN LNYDIIFTLE RFPEFHEKIN ARGAHFGLGG AAANTISWLA HFGLKTGYIG
AVGNDDVGEM HIKYFQGIGV DTGGIDVVEE PSGVAVAMVA GDDKRIVKYP GANLRRRFKP
EYASRAKFLH LSSNPPELIE EAVNFASQRG IKVSLDIGEA PLPRELESKV DYLMMNEDEY
RRKYGSLDPS LCRAKNLVVT LNGGGALVRE GDNVFEVRGL SAKVVDSTGA GDSFDAGVIY
GVLNGWSLLD SAKLGMLLAY LTVQKVGARS AIVPLEEVKR IAREVGLDLP FNRT
