NK_METTH
ID NK_METTH Reviewed; 309 AA.
AC O27587;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Nucleoside kinase {ECO:0000250|UniProtKB:Q57849};
DE Short=NK {ECO:0000250|UniProtKB:Q57849};
DE EC=2.7.1.- {ECO:0000250|UniProtKB:Q57849};
GN OrderedLocusNames=MTH_1544;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Catalyzes the phosphorylation of a wide range of nucleosides
CC to yield nucleoside monophosphates, using ATP, ITP or GTP as phosphate
CC donor. {ECO:0000250|UniProtKB:Q57849}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q57849};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q57849}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AE000666; AAB86018.1; -; Genomic_DNA.
DR PIR; A69073; A69073.
DR RefSeq; WP_010877153.1; NC_000916.1.
DR AlphaFoldDB; O27587; -.
DR SMR; O27587; -.
DR STRING; 187420.MTH_1544; -.
DR EnsemblBacteria; AAB86018; AAB86018; MTH_1544.
DR GeneID; 1471813; -.
DR KEGG; mth:MTH_1544; -.
DR PATRIC; fig|187420.15.peg.1507; -.
DR HOGENOM; CLU_027634_5_2_2; -.
DR OMA; SQQIARM; -.
DR Proteomes; UP000005223; 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; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="Nucleoside kinase"
FT /id="PRO_0000080154"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 110..112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 217..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
FT SITE 252
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q57849"
SQ SEQUENCE 309 AA; 33673 MW; A273E2DEBE3E4DD4 CRC64;
MSEDRDLLAV GHTAFDYIIH LDEFPEPNTS TAIKRMRNLH GGAAANVALV GSRLGLRTSL
VSAVGGDFEG SEYRELLESS GIDIESMILV ADESTPTAFV MTDSDHNQIS YFYWGAARYF
KDAETPADAI KSARAVHLAT GDPSFNCRCG EFARSLGKII SFDPGQDLHM YSRSQLERAV
GVCDILFGNH HEIDRICSKL SVDIHGLREM GPGVVVKTYG KEGSIIYSDD VIKIDAIPRE
AVDPTGAGDS YRAGFMRAYL RGADLKTCGR FASAVASFIV EDEGTQTNIP DTGEAVKRFT
AQWGYEPPI
