ID   NDKA1_XENLA             Reviewed;         154 AA.
AC   P70010; Q68FI7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 103.
DE   RecName: Full=Nucleoside diphosphate kinase A1;
DE            Short=NDK A1;
DE            Short=NDP kinase A1;
DE            EC=2.7.4.6;
DE   AltName: Full=NM23/nucleoside diphosphate kinase A1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RA   Ouatas T., Abdallah B., Gasmi L., Mazabraud A.;
RT   "Several genes encode the metastasis suppressor NM23/nucleoside diphosphate
RT   kinase of Xenopus laevis.";
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR   EMBL; X97900; CAA66474.1; -; mRNA.
DR   EMBL; BC079795; AAH79795.1; -; mRNA.
DR   RefSeq; XP_018095479.1; XM_018239990.2.
DR   RefSeq; XP_018095480.1; XM_018239991.2.
DR   RefSeq; XP_018095481.1; XM_018239992.2.
DR   AlphaFoldDB; P70010; -.
DR   SMR; P70010; -.
DR   DNASU; 394350; -.
DR   GeneID; 394350; -.
DR   AGR; Xenbase:XB-GENE-923251; -.
DR   CTD; 394350; -.
DR   Xenbase; XB-GENE-923251; nme2.L.
DR   OrthoDB; 2162449at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 394350; Expressed in oocyte and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   CDD; cd04413; NDPk_I; 1.
DR   FunFam; 3.30.70.141:FF:000039; Nucleoside diphosphate kinase B; 1.
DR   Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 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   NCBIfam; NF001908; PRK00668.1; 1.
DR   PANTHER; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1.
DR   PROSITE; PS00469; NDPK; 1.
DR   PROSITE; PS51374; NDPK_LIKE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..154
FT                   /note="Nucleoside diphosphate kinase A1"
FT                   /id="PRO_0000137120"
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   154 AA;  17489 MW;  DDE3A5621ADB6333 CRC64;
     MAANKERTFI AIKPDGVQRG LMGDIIKRFE QKGFRLVAMK FQQASQDLLR QHYIDLKDRP
     FYPGLVEYMS SGPVLAMVWE GLNVVKTGRV MLGETNPADS KPGTIRGDFC IQVGRNIIHG
     SDSVESANKE IALWFKDEEL VENKSCAYEW VYEN
//