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NDK_HELMI
ID   NDK_HELMI               Reviewed;         149 AA.
AC   B0TBN6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Helmi_12500;
GN   ORFNames=HM1_0677;
OS   Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliomicrobium.
OX   NCBI_TaxID=498761;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51547 / Ice1;
RX   PubMed=18441057; DOI=10.1128/jb.00299-08;
RA   Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA   Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA   Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA   Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT   "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT   of the Firmicutes containing the simplest photosynthetic apparatus.";
RL   J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ83875.1; -; Genomic_DNA.
DR   RefSeq; WP_012282393.1; NC_010337.2.
DR   AlphaFoldDB; B0TBN6; -.
DR   SMR; B0TBN6; -.
DR   STRING; 498761.HM1_0677; -.
DR   EnsemblBacteria; ABZ83875; ABZ83875; HM1_0677.
DR   KEGG; hmo:HM1_0677; -.
DR   eggNOG; COG0105; Bacteria.
DR   HOGENOM; CLU_060216_6_3_9; -.
DR   OMA; KIVAMKM; -.
DR   OrthoDB; 1752581at2; -.
DR   Proteomes; UP000008550; 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..149
FT                   /note="Nucleoside diphosphate kinase"
FT                   /id="PRO_1000192263"
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   149 AA;  16683 MW;  6E6E16045191E5C1 CRC64;
     MERTYLMIKP DGVQRGLVGE IISRFEKKGF KLVGMKFLRL TREMAEKHYA EHVGKPFFAG
     LVDYIISGPV VAMCWEGKDI VSVSREMMGA TNPAKAAPGT IRGTYAVDIG RNIIHGSDSP
     ASAERELAIY FQSDELVEWD RTLQGWLTE
 
 
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