ID   NDKB_MERHU              Reviewed;         128 AA.
AC   P85285;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 63.
DE   RecName: Full=Nucleoside diphosphate kinase B {ECO:0000250|UniProtKB:P22392};
DE            Short=NDP kinase B {ECO:0000250|UniProtKB:P22392};
DE            Short=NDPK B {ECO:0000250|UniProtKB:P22392};
DE            EC=2.7.4.6 {ECO:0000250|UniProtKB:P22392};
DE   AltName: Full=Histidine protein kinase NDKB;
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:P22392};
DE   AltName: Full=Nucleoside diphosphate kinases 2 {ECO:0000250|UniProtKB:P22392};
DE            Short=NDPK2 {ECO:0000250|UniProtKB:P22392};
DE   Flags: Fragments;
GN   Name=nme2 {ECO:0000250|UniProtKB:P22392};
OS   Merluccius hubbsi (Argentine hake) (Merluccius gayi hubbsi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Merlucciidae; Merluccius.
OX   NCBI_TaxID=89949;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
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: Catalyzes the transfer of a gamma-phosphoryl group from a
CC       nucleoside triphosphate, mainly ATP, to a nucleoside diphosphate via a
CC       ping-pong mechanism involving a phosphohistidine intermediate,
CC       therefore contributing to the nucleoside triphosphate homeostasis. Also
CC       functions as a histidine protein kinase by transferring the phosphoryl
CC       group from the phosphohistidine intermediate to a histidine residue in
CC       target proteins (By similarity). Additionally may be involved in
CC       transcriptional regulation through direct DNA binding and chromatin
CC       remodeling (By similarity). {ECO:0000250|UniProtKB:P22392}.
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:P22392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44641;
CC         Evidence={ECO:0000250|UniProtKB:P22392};
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:P22392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18114;
CC         Evidence={ECO:0000250|UniProtKB:P22392};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=IDP + ATP = ITP + ADP; Xref=Rhea:RHEA:30347,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58280, ChEBI:CHEBI:61402,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000250|UniProtKB:P22392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30348;
CC         Evidence={ECO:0000250|UniProtKB:P22392};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP + ATP = GTP + ADP; Xref=Rhea:RHEA:27686,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000250|UniProtKB:Q01768};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27687;
CC         Evidence={ECO:0000250|UniProtKB:Q01768};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP + ATP = ADP + ATP; Xref=Rhea:RHEA:84315,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P19804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84316;
CC         Evidence={ECO:0000250|UniProtKB:P19804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP + ATP = UTP + ADP; Xref=Rhea:RHEA:25098,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000250|UniProtKB:P19804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25099;
CC         Evidence={ECO:0000250|UniProtKB:P19804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP + ATP = CTP + ADP; Xref=Rhea:RHEA:25237,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:58069,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000250|UniProtKB:P19804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25238;
CC         Evidence={ECO:0000250|UniProtKB:P19804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP + ATP = dTTP + ADP; Xref=Rhea:RHEA:27682,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000250|UniProtKB:P22392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27683;
CC         Evidence={ECO:0000250|UniProtKB:P22392};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P22392};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P22392};
CC   -!- SUBUNIT: Homohexamer (By similarity). Heterohexamer of two different
CC       chains: A/NME1 and B/NME2 (A5B or A4B2 or A3B3 or A2B4 or AB5) (By
CC       similarity). {ECO:0000250|UniProtKB:P22392}.
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   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P22392}.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000255}.
CC   -!- CAUTION: Originnally, in addition to its DNA binding activity, some
CC       reports shown that exhibited an intrinsic nuclease activity (By
CC       similarity). However, this nuclease activity has not been confirmed (By
CC       similarity). {ECO:0000250|UniProtKB:P22392}.
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DR   AlphaFoldDB; P85285; -.
DR   SMR; P85285; -.
DR   iPTMnet; P85285; -.
DR   BRENDA; 2.7.4.6; 10452.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0004673; F:protein histidine kinase activity; ISS:UniProtKB.
DR   GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0072521; P:purine-containing compound metabolic process; IEA:UniProtKB-ARBA.
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   InterPro; IPR034907; NDK-like_dom.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   PANTHER; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR   Pfam; PF00334; NDK; 1.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1.
DR   PROSITE; PS51374; NDPK_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; 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..128
FT                   /note="Nucleoside diphosphate kinase B"
FT                   /id="PRO_0000306189"
FT   ACT_SITE        94
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P15531,
FT                   ECO:0000255|PROSITE-ProRule:PRU10030"
FT   BINDING         9
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:P22392"
FT   BINDING         9
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000250|UniProtKB:P22392"
FT   BINDING         31
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:P22392"
FT   BINDING         70
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:P22392"
FT   BINDING         70
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000250|UniProtKB:P22392"
FT   BINDING         91
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:P22392"
FT   BINDING         91
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000250|UniProtKB:P22392"
FT   BINDING         94
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:P22392"
FT   BINDING         128
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000250|UniProtKB:P22392"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:17622168"
FT   NON_CONS        23..24
FT                   /evidence="ECO:0000303|PubMed:17622168"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000303|PubMed:17622168"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000303|PubMed:17622168"
FT   NON_CONS        64..65
FT                   /evidence="ECO:0000303|PubMed:17622168"
SQ   SEQUENCE   128 AA;  14393 MW;  1EBA140A08C40E69 CRC64;
     MEQTFVAIKP DGVQRGLCGE VMKFIQPMKH YLDLKDMPFY AGLCKYMSSG PVFAMVWEGE
     GIVKMMLGET NPADSKPGSI RGDFCINIGR NIIHGSDTVE NAKMEVGLWF KPEEFVAYAE
     KAKAWVYE
//