NK_METJA
ID NK_METJA Reviewed; 302 AA.
AC Q57849;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Nucleoside kinase {ECO:0000303|PubMed:17021658};
DE Short=NK {ECO:0000303|PubMed:17021658};
DE AltName: Full=ATP-dependent nucleoside monophosphokinase {ECO:0000305};
DE AltName: Full=Cytidine kinase {ECO:0000303|PubMed:17021658};
DE EC=2.7.1.213 {ECO:0000269|PubMed:17021658};
DE AltName: Full=Guanosine-inosine kinase {ECO:0000303|PubMed:17021658};
DE EC=2.7.1.73 {ECO:0000269|PubMed:17021658};
GN OrderedLocusNames=MJ0406;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APOENZYME AND
RP IN COMPLEX WITH ATP ANALOG AND ADENOSINE, COFACTOR, MASS SPECTROMETRY,
RP SUBUNIT, REACTION MECHANISM, AND ACTIVE SITE.
RX PubMed=16929110; DOI=10.1107/s0907444906024826;
RA Arnfors L., Hansen T., Schonheit P., Ladenstein R., Meining W.;
RT "Structure of Methanocaldococcus jannaschii nucleoside kinase: an archaeal
RT member of the ribokinase family.";
RL Acta Crystallogr. D 62:1085-1097(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=17021658; DOI=10.1007/s00792-006-0018-1;
RA Hansen T., Arnfors L., Ladenstein R., Schoenheit P.;
RT "The phosphofructokinase-B (MJ0406) from Methanocaldococcus jannaschii
RT represents a nucleoside kinase with a broad substrate specificity.";
RL Extremophiles 11:105-114(2007).
CC -!- FUNCTION: Catalyzes the phosphorylation of a wide range of nucleosides
CC to yield nucleoside monophosphates. Shows the highest activity for
CC inosine, guanosine and cytidine, but very poor kinase activity with
CC adenosine, thymidine, uridine and xanthosine. ATP is the best phosphate
CC donor, but can also use ITP and GTP. Shows extremely low activity with
CC fructose-6-phosphate. {ECO:0000269|PubMed:17021658}.
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:17021658};
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:17021658};
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:17021658};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17021658, ECO:0000305|PubMed:16929110};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17021658};
CC Note=Can use Mg(2+) and Mn(2+) with equal efficiency in vitro, and to a
CC lesser extent, Ni(2+). {ECO:0000269|PubMed:17021658};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for ATP (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=17 uM for cytidine (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=20 uM for cytidine (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=20 uM for inosine (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=21 uM for inosine (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=62 uM for guanosine (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=78 uM for guanosine (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=160 uM for adenosine (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=180 uM for uridine (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=200 uM for uridine (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=230 uM for adenosine (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=300 uM for ribose (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=710 uM for xanthosine (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=900 uM for thymidine (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=1000 uM for thymidine (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=1800 uM for fructose (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=2200 uM for 2-deoxy-adenosine (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC KM=2500 uM for 2-deoxy-adenosine (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:17021658};
CC Vmax=120 umol/min/mg enzyme with guanosine as substrate (at 70
CC degrees Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=75 umol/min/mg enzyme with inosine as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=70 umol/min/mg enzyme with cytidine as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=29.3 umol/min/mg enzyme with guanosine as substrate (at 50
CC degrees Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=18.8 umol/min/mg enzyme with inosine as substrate (at 50 degrees
CC Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=9 umol/min/mg enzyme with cytidine as substrate (at 50 degrees
CC Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=4 umol/min/mg enzyme with adenosine as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=1 umol/min/mg enzyme with adenosine as substrate (at 50 degrees
CC Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=0.25 umol/min/mg enzyme with uridine as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=0.6 umol/min/mg enzyme with xanthosine as substrate (at 50
CC degrees Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=0.6 umol/min/mg enzyme with ribose as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=0.2 umol/min/mg enzyme with 2-deoxy-adenosine as substrate (at
CC 70 degrees Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=0.08 umol/min/mg enzyme with thymidine as substrate (at 70
CC degrees Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=0.05 umol/min/mg enzyme with 2-deoxy-adenosine as substrate (at
CC 50 degrees Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=0.04 umol/min/mg enzyme with uridine as substrate (at 50 degrees
CC Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=0.03 umol/min/mg enzyme with fructose as substrate (at 70
CC degrees Celsius) {ECO:0000269|PubMed:17021658};
CC Vmax=0.01 umol/min/mg enzyme with thymidine as substrate (at 50
CC degrees Celsius) {ECO:0000269|PubMed:17021658};
CC pH dependence:
CC Optimum pH is 7.0. 50% of activity is found at pH 6.1 and 8.2.
CC {ECO:0000269|PubMed:17021658};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius. Thermostable.
CC {ECO:0000269|PubMed:17021658};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16929110,
CC ECO:0000269|PubMed:17021658}.
CC -!- MASS SPECTROMETRY: Mass=33937; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16929110};
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB98396.1; -; Genomic_DNA.
DR PIR; F64350; F64350.
DR PDB; 2C49; X-ray; 1.92 A; A/B=1-302.
DR PDB; 2C4E; X-ray; 1.70 A; A=1-302.
DR PDBsum; 2C49; -.
DR PDBsum; 2C4E; -.
DR AlphaFoldDB; Q57849; -.
DR SMR; Q57849; -.
DR STRING; 243232.MJ_0406; -.
DR EnsemblBacteria; AAB98396; AAB98396; MJ_0406.
DR KEGG; mja:MJ_0406; -.
DR eggNOG; arCOG00014; Archaea.
DR HOGENOM; CLU_027634_5_2_2; -.
DR InParanoid; Q57849; -.
DR OMA; SQQIARM; -.
DR PhylomeDB; Q57849; -.
DR BRENDA; 2.7.1.B20; 3260.
DR EvolutionaryTrace; Q57849; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106366; F:guanosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008906; F:inosine kinase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0019206; F:nucleoside kinase activity; IDA:UniProtKB.
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; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Kinase; Magnesium;
KW Manganese; Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16929110"
FT CHAIN 2..302
FT /note="Nucleoside kinase"
FT /id="PRO_0000080152"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:16929110"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT BINDING 111..113
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT BINDING 214..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16929110,
FT ECO:0007744|PDB:2C49"
FT SITE 250
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:16929110"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:2C49"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2C4E"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2C49"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:2C4E"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:2C4E"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:2C4E"
SQ 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
