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Nucleoside kinase (NK) (ATP-dependent nucleoside monophosphokinase) (Cytidine kinase) (EC 2.7.1.213) (Guanosine kinase) (EC 2.7.1.-) (Inosine kinase) (EC 2.7.1.73)

 NK_METJA                Reviewed;         302 AA.
Q57849;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-JUL-2017, entry version 102.
RecName: Full=Nucleoside kinase {ECO:0000303|PubMed:17021658};
Short=NK {ECO:0000303|PubMed:17021658};
AltName: Full=ATP-dependent nucleoside monophosphokinase {ECO:0000305};
AltName: Full=Cytidine kinase {ECO:0000303|PubMed:17021658};
EC=2.7.1.213 {ECO:0000269|PubMed:17021658};
AltName: Full=Guanosine kinase {ECO:0000303|PubMed:17021658};
EC=2.7.1.- {ECO:0000269|PubMed:17021658};
AltName: Full=Inosine kinase {ECO:0000303|PubMed:17021658};
EC=2.7.1.73 {ECO:0000269|PubMed:17021658};
OrderedLocusNames=MJ0406;
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
Archaea; Euryarchaeota; Methanococci; Methanococcales;
Methanocaldococcaceae; Methanocaldococcus.
NCBI_TaxID=243232;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=8688087; DOI=10.1126/science.273.5278.1058;
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D.,
Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"Complete genome sequence of the methanogenic archaeon, Methanococcus
jannaschii.";
Science 273:1058-1073(1996).
[2]
PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APOENZYME
AND IN COMPLEX WITH ATP ANALOG AND ADENOSINE, COFACTOR, MASS
SPECTROMETRY, SUBUNIT, REACTION MECHANISM, AND ACTIVE SITE.
PubMed=16929110; DOI=10.1107/S0907444906024826;
Arnfors L., Hansen T., Schonheit P., Ladenstein R., Meining W.;
"Structure of Methanocaldococcus jannaschii nucleoside kinase: an
archaeal member of the ribokinase family.";
Acta Crystallogr. D 62:1085-1097(2006).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
SUBUNIT, AND SUBSTRATE SPECIFICITY.
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=17021658; DOI=10.1007/s00792-006-0018-1;
Hansen T., Arnfors L., Ladenstein R., Schoenheit P.;
"The phosphofructokinase-B (MJ0406) from Methanocaldococcus jannaschii
represents a nucleoside kinase with a broad substrate specificity.";
Extremophiles 11:105-114(2007).
-!- FUNCTION: Catalyzes the phosphorylation of a wide range of
nucleosides to yield nucleoside monophosphates. Shows the highest
activity for inosine, guanosine and cytidine, but very poor kinase
activity with adenosine, thymidine, uridine and xanthosine. ATP is
the best phosphate donor, but can also use ITP and GTP. Shows
extremely low activity with fructose-6-phosphate.
{ECO:0000269|PubMed:17021658}.
-!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP.
{ECO:0000269|PubMed:17021658}.
-!- CATALYTIC ACTIVITY: ATP + guanosine = ADP + GMP.
{ECO:0000269|PubMed:17021658}.
-!- CATALYTIC ACTIVITY: ATP + inosine = ADP + IMP.
{ECO:0000269|PubMed:17021658}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17021658,
ECO:0000305|PubMed:16929110};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17021658};
Note=Can use Mg(2+) and Mn(2+) with equal efficiency in vitro, and
to a lesser extent, Ni(2+). {ECO:0000269|PubMed:17021658};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.25 mM for ATP (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=17 uM for cytidine (at 50 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=20 uM for cytidine (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=20 uM for inosine (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=21 uM for inosine (at 50 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=62 uM for guanosine (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=78 uM for guanosine (at 50 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=160 uM for adenosine (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=180 uM for uridine (at 50 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=200 uM for uridine (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=230 uM for adenosine (at 50 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=300 uM for ribose (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=710 uM for xanthosine (at 50 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=900 uM for thymidine (at 50 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=1000 uM for thymidine (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=1800 uM for fructose (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=2200 uM for 2-deoxy-adenosine (at 70 degrees Celsius)
{ECO:0000269|PubMed:17021658};
KM=2500 uM for 2-deoxy-adenosine (at 50 degrees Celsius)
{ECO:0000269|PubMed:17021658};
Vmax=120 umol/min/mg enzyme with guanosine as substrate (at 70
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=75 umol/min/mg enzyme with inosine as substrate (at 70
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=70 umol/min/mg enzyme with cytidine as substrate (at 70
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=29.3 umol/min/mg enzyme with guanosine as substrate (at 50
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=18.8 umol/min/mg enzyme with inosine as substrate (at 50
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=9 umol/min/mg enzyme with cytidine as substrate (at 50
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=4 umol/min/mg enzyme with adenosine as substrate (at 70
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=1 umol/min/mg enzyme with adenosine as substrate (at 50
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=0.25 umol/min/mg enzyme with uridine as substrate (at 70
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=0.6 umol/min/mg enzyme with xanthosine as substrate (at 50
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=0.6 umol/min/mg enzyme with ribose as substrate (at 70
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=0.2 umol/min/mg enzyme with 2-deoxy-adenosine as substrate
(at 70 degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=0.08 umol/min/mg enzyme with thymidine as substrate (at 70
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=0.05 umol/min/mg enzyme with 2-deoxy-adenosine as substrate
(at 50 degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=0.04 umol/min/mg enzyme with uridine as substrate (at 50
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=0.03 umol/min/mg enzyme with fructose as substrate (at 70
degrees Celsius) {ECO:0000269|PubMed:17021658};
Vmax=0.01 umol/min/mg enzyme with thymidine as substrate (at 50
degrees Celsius) {ECO:0000269|PubMed:17021658};
pH dependence:
Optimum pH is 7.0. 50% of activity is found at pH 6.1 and 8.2.
{ECO:0000269|PubMed:17021658};
Temperature dependence:
Optimum temperature is 85 degrees Celsius. Thermostable.
{ECO:0000269|PubMed:17021658};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16929110,
ECO:0000269|PubMed:17021658}.
-!- MASS SPECTROMETRY: Mass=33937; Method=Electrospray; Range=2-302;
Evidence={ECO:0000269|PubMed:16929110};
-!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L77117; AAB98396.1; -; Genomic_DNA.
PIR; F64350; F64350.
PDB; 2C49; X-ray; 1.92 A; A/B=1-302.
PDB; 2C4E; X-ray; 1.70 A; A=1-302.
PDBsum; 2C49; -.
PDBsum; 2C4E; -.
ProteinModelPortal; Q57849; -.
SMR; Q57849; -.
STRING; 243232.MJ_0406; -.
EnsemblBacteria; AAB98396; AAB98396; MJ_0406.
KEGG; mja:MJ_0406; -.
eggNOG; arCOG00014; Archaea.
eggNOG; COG0524; LUCA.
InParanoid; Q57849; -.
OMA; GCQTNLP; -.
OrthoDB; POG093Z05O0; -.
PhylomeDB; Q57849; -.
BRENDA; 2.7.1.B20; 3260.
EvolutionaryTrace; Q57849; -.
Proteomes; UP000000805; Chromosome.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019200; F:carbohydrate kinase activity; IBA:GO_Central.
GO; GO:0008906; F:inosine kinase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0019206; F:nucleoside kinase activity; IDA:UniProtKB.
GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
Gene3D; 3.40.1190.20; -; 1.
InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
InterPro; IPR011611; PfkB_dom.
InterPro; IPR002139; Ribo/fructo_kinase.
InterPro; IPR029056; Ribokinase-like.
Pfam; PF00294; PfkB; 1.
PRINTS; PR00990; RIBOKINASE.
SUPFAM; SSF53613; SSF53613; 1.
PROSITE; PS00583; PFKB_KINASES_1; 1.
PROSITE; PS00584; PFKB_KINASES_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome;
Direct protein sequencing; Kinase; Magnesium; Manganese;
Nucleotide-binding; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:16929110}.
CHAIN 2 302 Nucleoside kinase.
/FTId=PRO_0000080152.
NP_BIND 214 219 ATP. {ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
REGION 111 113 Substrate binding. {ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
ACT_SITE 247 247 Proton acceptor.
{ECO:0000305|PubMed:16929110}.
BINDING 17 17 Substrate. {ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
BINDING 33 33 Substrate. {ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
BINDING 43 43 Substrate; via amide nitrogen.
{ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
BINDING 47 47 Substrate. {ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
BINDING 109 109 ATP. {ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
BINDING 163 163 Substrate. {ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
BINDING 186 186 ATP. {ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
BINDING 247 247 Substrate. {ECO:0000244|PDB:2C49,
ECO:0000269|PubMed:16929110}.
SITE 250 250 Transition state stabilizer.
{ECO:0000305|PubMed:16929110}.
STRAND 5 12 {ECO:0000244|PDB:2C4E}.
STRAND 15 21 {ECO:0000244|PDB:2C4E}.
STRAND 28 35 {ECO:0000244|PDB:2C49}.
STRAND 37 42 {ECO:0000244|PDB:2C4E}.
HELIX 44 54 {ECO:0000244|PDB:2C4E}.
STRAND 58 62 {ECO:0000244|PDB:2C4E}.
TURN 67 71 {ECO:0000244|PDB:2C4E}.
HELIX 73 80 {ECO:0000244|PDB:2C4E}.
STRAND 92 94 {ECO:0000244|PDB:2C4E}.
STRAND 98 103 {ECO:0000244|PDB:2C4E}.
STRAND 109 114 {ECO:0000244|PDB:2C49}.
HELIX 116 123 {ECO:0000244|PDB:2C4E}.
STRAND 131 136 {ECO:0000244|PDB:2C4E}.
HELIX 141 151 {ECO:0000244|PDB:2C4E}.
STRAND 155 159 {ECO:0000244|PDB:2C4E}.
HELIX 162 167 {ECO:0000244|PDB:2C4E}.
HELIX 170 178 {ECO:0000244|PDB:2C4E}.
STRAND 181 186 {ECO:0000244|PDB:2C4E}.
HELIX 187 197 {ECO:0000244|PDB:2C4E}.
HELIX 201 205 {ECO:0000244|PDB:2C4E}.
STRAND 209 214 {ECO:0000244|PDB:2C4E}.
HELIX 216 218 {ECO:0000244|PDB:2C4E}.
STRAND 220 223 {ECO:0000244|PDB:2C4E}.
STRAND 228 231 {ECO:0000244|PDB:2C4E}.
HELIX 245 258 {ECO:0000244|PDB:2C4E}.
HELIX 263 277 {ECO:0000244|PDB:2C4E}.
STRAND 280 284 {ECO:0000244|PDB:2C4E}.
HELIX 290 299 {ECO:0000244|PDB:2C4E}.
SEQUENCE 302 AA; 33920 MW; 6A535606CC7D3260 CRC64;
MGGKMEKITC VGHTALDYIF NVEKFPEPNT SIQIPSARKY YGGAAANTAV GIKKLGVNSE
LLSCVGYDFK NSGYERYLKN LDINISKLYY SEEEETPKAW IFTDKDNNQI TFFLWGAAKH
YKELNPPNFN TEIVHIATGD PEFNLKCAKK AYGNNLVSFD PGQDLPQYSK EMLLEIIEHT
NFLFMNKHEF ERASNLLNFE IDDYLERVDA LIVTKGSKGS VIYTKDKKIE IPCIKAGKVI
DPTGAGDSYR AGFLSAYVKG YDLEKCGLIG AATASFVVEA KGCQTNLPTW DKVVERLEKH
RI


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