NDKB_MERAA
ID NDKB_MERAA Reviewed; 128 AA.
AC P85288;
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 Merluccius australis australis (Austral hake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Merlucciidae; Merluccius.
OX NCBI_TaxID=307686;
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: 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; P85288; -.
DR SMR; P85288; -.
DR iPTMnet; P85288; -.
DR BRENDA; 2.7.4.6; 10455.
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:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.141; -; 1.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR Pfam; PF00334; NDK; 1.
DR SMART; SM00562; NDK; 1.
DR SUPFAM; SSF54919; SSF54919; 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_0000306184"
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="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15531"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15531"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15531"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15531"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15531"
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
