NK_THEAC
ID NK_THEAC Reviewed; 287 AA.
AC Q9HJT3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Nucleoside kinase {ECO:0000303|PubMed:23161756};
DE Short=NK {ECO:0000303|PubMed:23161756};
DE AltName: Full=Adenosine kinase {ECO:0000305|PubMed:23161756};
DE EC=2.7.1.20 {ECO:0000269|PubMed:23161756};
DE AltName: Full=Broad specificity nucleoside kinase {ECO:0000303|PubMed:23161756};
DE AltName: Full=Cytidine kinase {ECO:0000305|PubMed:23161756};
DE EC=2.7.1.213 {ECO:0000269|PubMed:23161756};
DE AltName: Full=Guanosine-inosine kinase {ECO:0000305|PubMed:23161756};
DE EC=2.7.1.73 {ECO:0000269|PubMed:23161756};
GN OrderedLocusNames=Ta0880 {ECO:0000312|EMBL:CAC12009.1};
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=23161756; DOI=10.1002/prot.24212;
RA Elkin S.R., Kumar A., Price C.W., Columbus L.;
RT "A broad specificity nucleoside kinase from Thermoplasma acidophilum.";
RL Proteins 81:568-582(2013).
CC -!- FUNCTION: Nucleoside kinase with broad substrate specificity. Catalyzes
CC the phosphorylation of a variety of nucleosides to the corresponding
CC nucleoside 5'-mono-phosphate in the presence of phosphate donors and
CC divalent cations. Displays the most efficient activity with guanosine,
CC followed by inosine, cytidine, and adenosine. Negligible enzymatic
CC activity is detected with thymidine, uridine, and 2-deoxyadenosine. ATP
CC is the most efficient phosphate donor, but can also use GTP and ITP.
CC Shows no sugar kinase activity, since it is unable to phosphorylate
CC ribose, fructose-1-phosphate, or fructose-6-phosphate.
CC {ECO:0000269|PubMed:23161756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + ATP = ADP + AMP + H(+); Xref=Rhea:RHEA:20824,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.20;
CC Evidence={ECO:0000269|PubMed:23161756};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.213;
CC Evidence={ECO:0000269|PubMed:23161756};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + guanosine = ADP + GMP + H(+); Xref=Rhea:RHEA:27710,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16750, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:456216; EC=2.7.1.73;
CC Evidence={ECO:0000269|PubMed:23161756};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + inosine = ADP + H(+) + IMP; Xref=Rhea:RHEA:21140,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17596, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456216; EC=2.7.1.73;
CC Evidence={ECO:0000269|PubMed:23161756};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23161756};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:23161756};
CC Note=Can use Mg(2+) and Co(2+) with equal efficiency in vitro, and to a
CC lesser extent, Mn(2+), but not Ni(2+). {ECO:0000269|PubMed:23161756};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.208 uM for guanosine (at pH 8.0 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:23161756};
CC KM=0.712 uM for inosine (at pH 8.0 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:23161756};
CC KM=0.411 uM for cytidine (at pH 8.0 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:23161756};
CC KM=1.12 uM for adenosine (at pH 8.0 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:23161756};
CC KM=46.9 uM for ATP (at pH 8.0 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:23161756};
CC KM=185 uM for GTP (at pH 8.0 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:23161756};
CC Note=kcat is 0.072 sec(-1) with ATP and guanosine as substrates. kcat
CC is 0.16 sec(-1) with ATP and inosine as substrates. kcat is 0.064
CC sec(-1) with ATP and cytidine as substrates. kcat is 0.084 sec(-1)
CC with ATP and adenosine as substrates. kcat is 0.27 sec(-1) with GTP
CC and inosine as substrates (at pH 8.0 and 22 degrees Celsius).
CC {ECO:0000269|PubMed:23161756};
CC pH dependence:
CC Optimum pH is 6.6. Significant activity is observed over the pH range
CC of 6.4 to 7.8. Enzymatic activity decreases markedly at pH 8.0 and at
CC pH 6.2 and below. {ECO:0000269|PubMed:23161756};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23161756}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AL445065; CAC12009.1; -; Genomic_DNA.
DR RefSeq; WP_010901290.1; NC_002578.1.
DR PDB; 3BF5; X-ray; 1.91 A; A/B=1-287.
DR PDBsum; 3BF5; -.
DR AlphaFoldDB; Q9HJT3; -.
DR SMR; Q9HJT3; -.
DR STRING; 273075.Ta0880; -.
DR DNASU; 1456419; -.
DR EnsemblBacteria; CAC12009; CAC12009; CAC12009.
DR GeneID; 1456419; -.
DR KEGG; tac:Ta0880; -.
DR eggNOG; arCOG00014; Archaea.
DR HOGENOM; CLU_027634_5_2_2; -.
DR OMA; SQQIARM; -.
DR OrthoDB; 98664at2157; -.
DR BRENDA; 2.7.1.B20; 6324.
DR EvolutionaryTrace; Q9HJT3; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0004001; F:adenosine kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0043771; F:cytidine kinase activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:1905108; F:guanosine binding; IDA:UniProtKB.
DR GO; GO:0106366; F:guanosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008906; F:inosine kinase activity; IDA:UniProtKB.
DR GO; GO:0019206; F:nucleoside kinase activity; IDA:UniProtKB.
DR GO; GO:0046085; P:adenosine metabolic process; IDA:UniProtKB.
DR GO; GO:0046087; P:cytidine metabolic process; IDA:UniProtKB.
DR GO; GO:0008617; P:guanosine metabolic process; IDA:UniProtKB.
DR GO; GO:0046102; P:inosine metabolic process; IDA:UniProtKB.
DR GO; GO:1901293; P:nucleoside phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR Gene3D; 2.20.150.10; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR023314; Myo_inos_IolC-like_sf.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cobalt; GTP-binding; Kinase; Magnesium;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..287
FT /note="Nucleoside kinase"
FT /id="PRO_0000439948"
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 196..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT SITE 230
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:3BF5"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3BF5"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 243..260
FT /evidence="ECO:0007829|PDB:3BF5"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:3BF5"
SQ SEQUENCE 287 AA; 32805 MW; 24CF1E8CE10466F8 CRC64;
MRFLAYFGHL NIDVLISVDS IPREGSVNVK DLRPRFGGTA GNFAIVAQKF RIPFDLYSAV
GMKTHREYLA MIESMGINTG HVEKFEDESG PICYIATDGK KQVSFMHQGA MEKWKPQLAD
EYEYVHFSTG PNYLDMAKSI RSKIIFDPSQ EIHKYSKDEL KKFHEISYMS IFNDHEYRVF
REMTGLSSPK VTTIVTNGER GSSLFMDGKK YDFPAIPSSG DTVGAGDSFR AGLYLALYNR
RSIEKGMIYG TIIAHHVIDD GIENFSLNME DLERETENYR RMFTKRS
