ID   NDK_COLLI               Reviewed;         153 AA.
AC   Q90380;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Nucleoside diphosphate kinase;
DE            Short=NDK;
DE            Short=NDP kinase;
DE            EC=2.7.4.6;
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9305928; DOI=10.1074/jbc.272.39.24604;
RA   Lambeth D.O., Mehus J.G., Ivey M.A., Milavetz B.I.;
RT   "Characterization and cloning of a nucleoside-diphosphate kinase targeted
RT   to matrix of mitochondria in pigeon.";
RL   J. Biol. Chem. 272:24604-24611(1997).
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; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane.
CC   -!- TISSUE SPECIFICITY: Highest levels in the liver and kidney with lower
CC       levels in the heart, brain and breast muscle.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR   EMBL; U61287; AAC60275.1; -; mRNA.
DR   EMBL; AF018266; AAC78437.1; -; Genomic_DNA.
DR   RefSeq; NP_001269739.1; NM_001282810.1.
DR   AlphaFoldDB; Q90380; -.
DR   SMR; Q90380; -.
DR   STRING; 8932.XP_005503167.1; -.
DR   GeneID; 102089990; -.
DR   KEGG; clv:102089990; -.
DR   eggNOG; KOG0888; Eukaryota.
DR   OrthoDB; 1334716at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Cytoplasm; Kinase; Magnesium; Membrane;
KW   Metal-binding; Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW   Transferase.
FT   CHAIN           1..153
FT                   /note="Nucleoside diphosphate kinase"
FT                   /id="PRO_0000137122"
FT   ACT_SITE        119
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   153 AA;  17299 MW;  4E245D7AE9F0C9EF CRC64;
     MAANCERTFI AIKPDGVQRG LVGEIIKRFE QKGFRLVGMK FVHASEELLK QHYIDLKDRP
     FYPGLVKYMN SGPIVAMVWE GLNVVKTGRV MLGETNPADS KPGTIRGDFC IQVGRNIIHG
     SDSVESAQKE INLWFKPAEL IDFKSCAHDW IYE