AC   MF_00451;
DC   Protein; auto
TR   HAMAP; MF_00451; -; 1; level=0
XX
Names: NDP_kinase
XX
ID   NDK
DE   RecName: Full=Nucleoside diphosphate kinase;
DE            Short=NDK;
DE            Short=NDP kinase;
DE            EC=2.7.4.6;
DE   AltName: Full=Nucleoside-2-P kinase;
GN   Name=ndk;
XX
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.
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;
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
case <OC:Bacteria>
CC   -!- SUBUNIT: Homotetramer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the NDK family.
XX
DR   Pfam; PF00334; NDK; 1; trigger=no
DR   PRINTS; PR01243; NUCDPKINASE; 1; trigger=no
DR   PROSITE; PS00469; NDP_KINASES; 1; trigger=no
DR   PROSITE; PS51374; NDPK_LIKE; 1; trigger=yes
XX
KW   Cytoplasm
KW   Magnesium
KW   Metal-binding
KW   Nucleotide metabolism
KW   Nucleotide-binding
KW   Phosphoprotein
KW   Transferase
KW   Kinase
KW   ATP-binding
case <FT:8> or <FT:9>
KW   Phosphoprotein
end case
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004550; F:nucleoside diphosphate kinase activity
GO   GO:0006241; P:CTP biosynthetic process
GO   GO:0006183; P:GTP biosynthetic process
GO   GO:0006228; P:UTP biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: NDK_ECOLI (P0A763)
FT   ACT_SITE        117
FT                   /note="Pros-phosphohistidine intermediate"
FT   Condition: H
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
FT   BINDING         59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [FY]
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: T
FT   BINDING         104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: N
FT   From: NDK_BACSU (P31103)
case <OC:Bacillaceae>
FT   MOD_RES         92
FT                   /note="Phosphothreonine"
FT   Condition: T
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT   Condition: S
end case
XX
Size: 133-174;
Related: None;
Template: P0A763; Q59636; O85501; P61136;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in PARUW
Plasmid: None
Comments: BORBU and PYRAE are divergent; not shown in alignment
XX
# Revision 1.44 2024/01/10
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