NDK_CHICK
ID NDK_CHICK Reviewed; 153 AA.
AC O57535;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Nucleoside diphosphate kinase;
DE Short=NDK;
DE Short=NDP kinase;
DE EC=2.7.4.6;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Mehus J.G., Lambeth D.O.;
RL Submitted (JAN-1998) 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 (By similarity). {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; AF043542; AAB99856.1; -; mRNA.
DR RefSeq; NP_990378.1; NM_205047.1.
DR AlphaFoldDB; O57535; -.
DR SMR; O57535; -.
DR BioGRID; 676189; 2.
DR IntAct; O57535; 1.
DR STRING; 9031.ENSGALP00000034078; -.
DR PaxDb; O57535; -.
DR Ensembl; ENSGALT00000034721; ENSGALP00000034078; ENSGALG00000002932.
DR GeneID; 395916; -.
DR KEGG; gga:395916; -.
DR CTD; 4831; -.
DR VEuPathDB; HostDB:geneid_395916; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000161569; -.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; O57535; -.
DR OMA; ALWFGEQ; -.
DR OrthoDB; 1334716at2759; -.
DR PhylomeDB; O57535; -.
DR TreeFam; TF106373; -.
DR PRO; PR:O57535; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000002932; Expressed in granulocyte and 14 other tissues.
DR ExpressionAtlas; O57535; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; ISS:AgBase.
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:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:AgBase.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:AgBase.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0045682; P:regulation of epidermis development; ISS:AgBase.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..153
FT /note="Nucleoside diphosphate kinase"
FT /id="PRO_0000250203"
FT ACT_SITE 119
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 89
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 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 153 AA; 17288 MW; 939DDD61D329E008 CRC64;
MAANCERTFI AIKPDGVQRG LVGEIIKRFE QKGFRLVAMK FVHASEDLLK QHYIDLKDRP
FYPGLVKYMN SGPVVAMVWE GLNVVKTGRV MLGETNPADS KPGTIRGDFC IQVGRNIIHG
SDSVESAQKE ISLWFKPAEL IDYRSCAHDW VYE
