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NDK_EXISA
ID   NDK_EXISA               Reviewed;         139 AA.
AC   C4L6N1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Nucleoside diphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00451};
DE            Short=NDK {ECO:0000255|HAMAP-Rule:MF_00451};
DE            Short=NDP kinase {ECO:0000255|HAMAP-Rule:MF_00451};
DE            EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_00451};
DE   AltName: Full=Nucleoside-2-P kinase {ECO:0000255|HAMAP-Rule:MF_00451};
GN   Name=ndk {ECO:0000255|HAMAP-Rule:MF_00451}; OrderedLocusNames=EAT1b_2996;
OS   Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium;
OC   unclassified Exiguobacterium.
OX   NCBI_TaxID=360911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1283 / AT1b;
RX   PubMed=21460088; DOI=10.1128/jb.00303-11;
RA   Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina del Rio T.,
RA   Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA   Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA   Hendrix C., Richardson P., Tiedje J.M.;
RT   "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT   AT1b.";
RL   J. Bacteriol. 193:2880-2881(2011).
CC   -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other
CC       than ATP. The ATP gamma phosphate is transferred to the NDP beta
CC       phosphate via a ping-pong mechanism, using a phosphorylated active-site
CC       intermediate. {ECO:0000255|HAMAP-Rule:MF_00451}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC         deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC         triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00451};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00451};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00451}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00451}.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000255|HAMAP-
CC       Rule:MF_00451}.
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DR   EMBL; CP001615; ACQ71910.1; -; Genomic_DNA.
DR   RefSeq; WP_015881469.1; NC_012673.1.
DR   AlphaFoldDB; C4L6N1; -.
DR   SMR; C4L6N1; -.
DR   STRING; 360911.EAT1b_2996; -.
DR   EnsemblBacteria; ACQ71910; ACQ71910; EAT1b_2996.
DR   KEGG; eat:EAT1b_2996; -.
DR   eggNOG; COG0105; Bacteria.
DR   HOGENOM; CLU_060216_6_3_9; -.
DR   OMA; KIVAMKM; -.
DR   OrthoDB; 1752581at2; -.
DR   Proteomes; UP000000716; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.141; -; 1.
DR   HAMAP; MF_00451; NDP_kinase; 1.
DR   InterPro; IPR034907; NDK-like_dom.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; SSF54919; 1.
DR   PROSITE; PS00469; NDP_KINASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..139
FT                   /note="Nucleoside diphosphate kinase"
FT                   /id="PRO_1000206211"
FT   ACT_SITE        115
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         9
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
SQ   SEQUENCE   139 AA;  15371 MW;  10D04E194696DFDA CRC64;
     MEKTFLMVKP DGVKRGLIGE IISRFENKGY TLNRLEMVTP SVEVAEAHYA EHKEKPFFGE
     LVEFLTSGPV VAMEWEGEDI VAVSRLMIGK TKPVDAQPGT IRGDFASTMS QNVIHGSDSV
     DSAERELSLW FAEVASHVS
 
 
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