NDKA2_BOVIN
ID NDKA2_BOVIN Reviewed; 152 AA.
AC P52175;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Nucleoside diphosphate kinase A 2;
DE Short=NDK A 2;
DE Short=NDP kinase A 2;
DE EC=2.7.4.6;
DE AltName: Full=Nucleoside diphosphate kinase NBR-B;
DE Short=NDK NBR-B;
GN Name=NME1-2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-152, CATALYTIC ACTIVITY,
RP SUBUNIT, SUBCELLULAR LOCATION, BLOCKAGE OF N-TERMINUS, AND X-RAY
RP CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC TISSUE=Retina;
RX PubMed=9760230; DOI=10.1021/bi980853s;
RA Abdulaev N.G., Karaschuk G.N., Ladner J.E., Kakuev D.L., Yakhyaev A.V.,
RA Tordova M., Gaidarov I.O., Popov V.I., Fujiwara J.H., Chinchilla D.,
RA Eisenstein E., Gilliland G.L., Ridge K.D.;
RT "Nucleoside diphosphate kinase from bovine retina: purification,
RT subcellular localization, molecular cloning, and three-dimensional
RT structure.";
RL Biochemistry 37:13958-13967(1998).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other
CC than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-
CC specific protein kinase, geranyl and farnesyl pyrophosphate kinase,
CC histidine protein kinase and 3'-5' exonuclease activities. Involved in
CC cell proliferation, differentiation and development, signal
CC transduction, G protein-coupled receptor endocytosis, and gene
CC expression. Required for neural development including neural patterning
CC and cell fate determination.
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:0000269|PubMed:9760230};
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:0000269|PubMed:9760230};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Autophosphorylation at His-118 increases
CC serine/threonine protein kinase activity of the enzyme. Interaction
CC with the SET complex inhibits exonuclease activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:9760230}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9760230}. Cell
CC membrane {ECO:0000269|PubMed:9760230}. Nucleus {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; X92957; CAA63533.1; -; mRNA.
DR PDB; 1BE4; X-ray; 2.40 A; A/B/C=2-152.
DR PDBsum; 1BE4; -.
DR AlphaFoldDB; P52175; -.
DR SMR; P52175; -.
DR STRING; 9913.ENSBTAP00000006106; -.
DR PRIDE; P52175; -.
DR Ensembl; ENSBTAT00000006106; ENSBTAP00000006106; ENSBTAG00000004651.
DR VEuPathDB; HostDB:ENSBTAG00000004651; -.
DR GeneTree; ENSGT00940000162213; -.
DR InParanoid; P52175; -.
DR OMA; KIVAMKM; -.
DR EvolutionaryTrace; P52175; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000004651; Expressed in retina and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004536; F:deoxyribonuclease activity; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.141; -; 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 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Differentiation;
KW Direct protein sequencing; Endocytosis; Kinase; Magnesium; Membrane;
KW Metal-binding; Neurogenesis; Nucleotide metabolism; Nucleotide-binding;
KW Nucleus; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9760230"
FT CHAIN 2..152
FT /note="Nucleoside diphosphate kinase A 2"
FT /id="PRO_0000137112"
FT ACT_SITE 118
FT /note="Pros-phosphohistidine intermediate"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:1BE4"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1BE4"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:1BE4"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:1BE4"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1BE4"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1BE4"
SQ SEQUENCE 152 AA; 17298 MW; F710E1DFC731B04B CRC64;
MANSERTFIA IKPDGVQRGL MGEIIKRFEQ KGFRLVAMKF MRASEDLLKE HYIDLKDRPF
FAGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVESAEKEI ALWFRPEELV NYKSCAQNWI YE
