ID   NDKB_MACNO              Reviewed;         126 AA.
AC   P85291;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Nucleoside diphosphate kinase B;
DE            Short=NDK B;
DE            Short=NDP kinase B;
DE            EC=2.7.4.6;
DE   Flags: Fragments;
GN   Name=nme2;
OS   Macruronus novaezelandiae (Blue grenadier) (Macruronus novaezelandiae
OS   novaezelandiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Merlucciidae; Macruronus.
OX   NCBI_TaxID=248764;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=White muscle {ECO:0000269|PubMed:17622168};
RX   PubMed=17622168; DOI=10.1021/pr0701963;
RA   Carrera M., Canas B., Pineiro C., Vazquez J., Gallardo J.M.;
RT   "De novo mass spectrometry sequencing and characterization of species-
RT   specific peptides from nucleoside diphosphate kinase B for the
RT   classification of commercial fish species belonging to the family
RT   Merlucciidae.";
RL   J. Proteome Res. 6:3070-3080(2007).
CC   -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other
CC       than ATP. {ECO:0000250|UniProtKB:P15531}.
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         Evidence={ECO:0000250|UniProtKB:P15531, 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:0000250|UniProtKB:P15531, ECO:0000255|PROSITE-
CC         ProRule:PRU10030};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P15531};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22392}. Nucleus
CC       {ECO:0000250|UniProtKB:P22392}. Cell projection, lamellipodium
CC       {ECO:0000250|UniProtKB:P22392}. Cell projection, ruffle
CC       {ECO:0000250|UniProtKB:P22392}.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000255}.
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DR   AlphaFoldDB; P85291; -.
DR   SMR; P85291; -.
DR   PRIDE; P85291; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001726; C:ruffle; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
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   InterPro; IPR034907; NDK-like_dom.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; SSF54919; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell projection; Cytoplasm;
KW   Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Transferase.
FT   CHAIN           <1..126
FT                   /note="Nucleoside diphosphate kinase B"
FT                   /id="PRO_0000306183"
FT   ACT_SITE        92
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P15531,
FT                   ECO:0000255|PROSITE-ProRule:PRU10030"
FT   BINDING         6
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15531"
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15531"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15531"
FT   BINDING         79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15531"
FT   BINDING         89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15531"
FT   NON_CONS        20..21
FT                   /evidence="ECO:0000303|PubMed:17622168"
FT   NON_CONS        24..25
FT                   /evidence="ECO:0000303|PubMed:17622168"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000303|PubMed:17622168"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:17622168"
SQ   SEQUENCE   126 AA;  14118 MW;  C836BD599663F83A CRC64;
     TFIAIKPDGV QRGLCGEVMK FIQPMKQHYL DLKDMPFYAG LCKYMASGPV FAMVWEGEGI
     VKMMLGETNP ADSKPGSIRG DFCINIGRNI IHGSDTLENA KMEIGLWFKG EEFVAYAEKA
     KAWVYE