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Nucleoside kinase (NK) (Adenosine kinase) (EC 2.7.1.20) (Broad specificity nucleoside kinase) (Cytidine kinase) (EC 2.7.1.213) (Guanosine kinase) (EC 2.7.1.-) (Inosine kinase) (EC 2.7.1.73)

 NK_THEAC                Reviewed;         287 AA.
Q9HJT3;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
10-OCT-2018, entry version 83.
RecName: Full=Nucleoside kinase {ECO:0000303|PubMed:23161756};
Short=NK {ECO:0000303|PubMed:23161756};
AltName: Full=Adenosine kinase {ECO:0000305|PubMed:23161756};
EC=2.7.1.20 {ECO:0000269|PubMed:23161756};
AltName: Full=Broad specificity nucleoside kinase {ECO:0000303|PubMed:23161756};
AltName: Full=Cytidine kinase {ECO:0000305|PubMed:23161756};
EC=2.7.1.213 {ECO:0000269|PubMed:23161756};
AltName: Full=Guanosine kinase {ECO:0000305|PubMed:23161756};
EC=2.7.1.- {ECO:0000269|PubMed:23161756};
AltName: Full=Inosine kinase {ECO:0000305|PubMed:23161756};
EC=2.7.1.73 {ECO:0000269|PubMed:23161756};
OrderedLocusNames=Ta0880 {ECO:0000312|EMBL:CAC12009.1};
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 /
NBRC 15155 / AMRC-C165).
Archaea; Euryarchaeota; Diaforarchaea group; Thermoplasmata;
Thermoplasmatales; Thermoplasmataceae; Thermoplasma.
NCBI_TaxID=273075;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
PubMed=11029001; DOI=10.1038/35035069;
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
"The genome sequence of the thermoacidophilic scavenger Thermoplasma
acidophilum.";
Nature 407:508-513(2000).
[2]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, AND
SUBUNIT.
STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
PubMed=23161756; DOI=10.1002/prot.24212;
Elkin S.R., Kumar A., Price C.W., Columbus L.;
"A broad specificity nucleoside kinase from Thermoplasma
acidophilum.";
Proteins 81:568-582(2013).
-!- FUNCTION: Nucleoside kinase with broad substrate specificity.
Catalyzes the phosphorylation of a variety of nucleosides to the
corresponding nucleoside 5'-mono-phosphate in the presence of
phosphate donors and divalent cations. Displays the most efficient
activity with guanosine, followed by inosine, cytidine, and
adenosine. Negligible enzymatic activity is detected with
thymidine, uridine, and 2-deoxyadenosine. ATP is the most
efficient phosphate donor, but can also use GTP and ITP. Shows no
sugar kinase activity, since it is unable to phosphorylate ribose,
fructose-1-phosphate, or fructose-6-phosphate.
{ECO:0000269|PubMed:23161756}.
-!- CATALYTIC ACTIVITY: ATP + adenosine = ADP + AMP.
{ECO:0000269|PubMed:23161756}.
-!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP.
{ECO:0000269|PubMed:23161756}.
-!- CATALYTIC ACTIVITY: ATP + guanosine = ADP + GMP.
{ECO:0000269|PubMed:23161756}.
-!- CATALYTIC ACTIVITY: ATP + inosine = ADP + IMP.
{ECO:0000269|PubMed:23161756}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:23161756};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:23161756};
Note=Can use Mg(2+) and Co(2+) with equal efficiency in vitro, and
to a lesser extent, Mn(2+), but not Ni(2+).
{ECO:0000269|PubMed:23161756};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.208 uM for guanosine (at pH 8.0 and 22 degrees Celsius)
{ECO:0000269|PubMed:23161756};
KM=0.712 uM for inosine (at pH 8.0 and 22 degrees Celsius)
{ECO:0000269|PubMed:23161756};
KM=0.411 uM for cytidine (at pH 8.0 and 22 degrees Celsius)
{ECO:0000269|PubMed:23161756};
KM=1.12 uM for adenosine (at pH 8.0 and 22 degrees Celsius)
{ECO:0000269|PubMed:23161756};
KM=46.9 uM for ATP (at pH 8.0 and 22 degrees Celsius)
{ECO:0000269|PubMed:23161756};
KM=185 uM for GTP (at pH 8.0 and 22 degrees Celsius)
{ECO:0000269|PubMed:23161756};
Note=kcat is 0.072 sec(-1) with ATP and guanosine as substrates.
kcat is 0.16 sec(-1) with ATP and inosine as substrates. kcat is
0.064 sec(-1) with ATP and cytidine as substrates. kcat is 0.084
sec(-1) with ATP and adenosine as substrates. kcat is 0.27 sec(-
1) with GTP and inosine as substrates (at pH 8.0 and 22 degrees
Celsius). {ECO:0000269|PubMed:23161756};
pH dependence:
Optimum pH is 6.6. Significant activity is observed over the pH
range of 6.4 to 7.8. Enzymatic activity decreases markedly at pH
8.0 and at pH 6.2 and below. {ECO:0000269|PubMed:23161756};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23161756}.
-!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AL445065; CAC12009.1; -; Genomic_DNA.
RefSeq; WP_010901290.1; NC_002578.1.
PDB; 3BF5; X-ray; 1.91 A; A/B=1-287.
PDBsum; 3BF5; -.
ProteinModelPortal; Q9HJT3; -.
SMR; Q9HJT3; -.
STRING; 273075.Ta0880; -.
DNASU; 1456419; -.
EnsemblBacteria; CAC12009; CAC12009; CAC12009.
GeneID; 1456419; -.
KEGG; tac:Ta0880; -.
eggNOG; arCOG00014; Archaea.
eggNOG; COG0524; LUCA.
HOGENOM; HOG000142559; -.
KO; K22026; -.
OMA; HLATGDP; -.
OrthoDB; POG093Z05O0; -.
BioCyc; TACI273075:G1GT7-977-MONOMER; -.
BRENDA; 2.7.1.B20; 6324.
EvolutionaryTrace; Q9HJT3; -.
Proteomes; UP000001024; Chromosome.
GO; GO:0004001; F:adenosine kinase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0043771; F:cytidine kinase activity; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:1905108; F:guanosine binding; IDA:UniProtKB.
GO; GO:0008906; F:inosine kinase activity; IDA:UniProtKB.
GO; GO:0019206; F:nucleoside kinase activity; IDA:UniProtKB.
GO; GO:0046085; P:adenosine metabolic process; IDA:UniProtKB.
GO; GO:0046087; P:cytidine metabolic process; IDA:UniProtKB.
GO; GO:0008617; P:guanosine metabolic process; IDA:UniProtKB.
GO; GO:0046102; P:inosine metabolic process; IDA:UniProtKB.
GO; GO:1901293; P:nucleoside phosphate biosynthetic process; IDA:UniProtKB.
GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
Gene3D; 2.20.150.10; -; 2.
Gene3D; 3.40.1190.20; -; 3.
InterPro; IPR023314; Myo_inos_iolC-like_sf.
InterPro; IPR011611; PfkB_dom.
InterPro; IPR029056; Ribokinase-like.
Pfam; PF00294; PfkB; 1.
SUPFAM; SSF53613; SSF53613; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cobalt; Complete proteome; GTP-binding;
Kinase; Magnesium; Nucleotide-binding; Reference proteome;
Transferase.
CHAIN 1 287 Nucleoside kinase.
/FTId=PRO_0000439948.
NP_BIND 196 201 ATP. {ECO:0000250|UniProtKB:Q57849}.
ACT_SITE 227 227 Proton acceptor.
{ECO:0000250|UniProtKB:Q57849}.
BINDING 13 13 Substrate.
{ECO:0000250|UniProtKB:Q57849}.
BINDING 28 28 Substrate.
{ECO:0000250|UniProtKB:Q57849}.
BINDING 38 38 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:Q57849}.
BINDING 42 42 Substrate.
{ECO:0000250|UniProtKB:Q57849}.
BINDING 102 102 ATP. {ECO:0000250|UniProtKB:Q57849}.
BINDING 104 104 Substrate.
{ECO:0000250|UniProtKB:Q57849}.
BINDING 150 150 Substrate.
{ECO:0000250|UniProtKB:Q57849}.
BINDING 173 173 ATP. {ECO:0000250|UniProtKB:Q57849}.
BINDING 227 227 Substrate.
{ECO:0000250|UniProtKB:Q57849}.
SITE 230 230 Transition state stabilizer.
{ECO:0000250|UniProtKB:Q57849}.
STRAND 2 7 {ECO:0000244|PDB:3BF5}.
STRAND 11 17 {ECO:0000244|PDB:3BF5}.
STRAND 23 28 {ECO:0000244|PDB:3BF5}.
STRAND 30 37 {ECO:0000244|PDB:3BF5}.
HELIX 38 49 {ECO:0000244|PDB:3BF5}.
STRAND 55 61 {ECO:0000244|PDB:3BF5}.
TURN 62 64 {ECO:0000244|PDB:3BF5}.
HELIX 66 74 {ECO:0000244|PDB:3BF5}.
STRAND 82 85 {ECO:0000244|PDB:3BF5}.
STRAND 91 97 {ECO:0000244|PDB:3BF5}.
STRAND 102 107 {ECO:0000244|PDB:3BF5}.
HELIX 110 113 {ECO:0000244|PDB:3BF5}.
STRAND 122 127 {ECO:0000244|PDB:3BF5}.
STRAND 129 132 {ECO:0000244|PDB:3BF5}.
HELIX 133 139 {ECO:0000244|PDB:3BF5}.
STRAND 142 146 {ECO:0000244|PDB:3BF5}.
HELIX 149 154 {ECO:0000244|PDB:3BF5}.
HELIX 157 166 {ECO:0000244|PDB:3BF5}.
STRAND 168 173 {ECO:0000244|PDB:3BF5}.
HELIX 174 184 {ECO:0000244|PDB:3BF5}.
STRAND 193 197 {ECO:0000244|PDB:3BF5}.
HELIX 198 200 {ECO:0000244|PDB:3BF5}.
STRAND 201 206 {ECO:0000244|PDB:3BF5}.
STRAND 209 214 {ECO:0000244|PDB:3BF5}.
HELIX 225 238 {ECO:0000244|PDB:3BF5}.
HELIX 243 260 {ECO:0000244|PDB:3BF5}.
HELIX 269 282 {ECO:0000244|PDB:3BF5}.
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


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