ID   NDK6_XENTR              Reviewed;         179 AA.
AC   B3DL53;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Nucleoside diphosphate kinase 6;
DE            Short=NDK 6;
DE            Short=NDP kinase 6;
DE            EC=2.7.4.6;
GN   Name=nme6;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2008) 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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10030};
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|PROSITE-ProRule:PRU10030};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR   EMBL; BC167315; AAI67315.1; -; mRNA.
DR   RefSeq; NP_001123709.1; NM_001130237.1.
DR   RefSeq; XP_012814101.1; XM_012958647.2.
DR   RefSeq; XP_017947439.1; XM_018091950.1.
DR   AlphaFoldDB; B3DL53; -.
DR   SMR; B3DL53; -.
DR   PaxDb; B3DL53; -.
DR   Ensembl; ENSXETT00000034257; ENSXETP00000034257; ENSXETG00000015714.
DR   GeneID; 100170458; -.
DR   KEGG; xtr:100170458; -.
DR   CTD; 10201; -.
DR   Xenbase; XB-GENE-969918; nme6.
DR   eggNOG; KOG0888; Eukaryota.
DR   HOGENOM; CLU_060216_8_0_1; -.
DR   InParanoid; B3DL53; -.
DR   OMA; QKWRRLM; -.
DR   OrthoDB; 1395365at2759; -.
DR   PhylomeDB; B3DL53; -.
DR   TreeFam; TF354225; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000015714; Expressed in egg cell and 12 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0030308; P:negative regulation of cell growth; IBA:GO_Central.
DR   GO; GO:0045839; P:negative regulation of mitotic nuclear division; IBA:GO_Central.
DR   GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   CDD; cd04414; NDPk6; 1.
DR   Gene3D; 3.30.70.141; -; 1.
DR   InterPro; IPR034907; NDK-like_dom.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   InterPro; IPR037994; NDPk6.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR   PANTHER; PTHR46956; PTHR46956; 1.
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; Kinase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..179
FT                   /note="Nucleoside diphosphate kinase 6"
FT                   /id="PRO_0000369547"
FT   ACT_SITE        128
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10030"
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
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         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   179 AA;  21027 MW;  C2AC7D0472CD10B2 CRC64;
     MSSFRWVRPL QLTLALIKPD AVANPVISEA VHQKILENNF LIIRHKELHW RSTDSQRFYC
     EHKGRFFYQR LVEFMSSGPM QAYILAHEDA VQLWRNLMGP TKVFRARIVA PGTVRGDLGL
     TDTRNTTHGS DSVESACREI TFFFPEFNTS DWYEKQEPRY RTGPVFYDEE RSEHRLEGE