NDK2_PSEMZ
ID NDK2_PSEMZ Reviewed; 27 AA.
AC P85930;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Nucleoside diphosphate kinase 2 {ECO:0000250|UniProtKB:Q02254, ECO:0000303|PubMed:18602030};
DE EC=2.7.4.6;
DE AltName: Full=Nucleoside diphosphate kinase II {ECO:0000250|UniProtKB:Q02254, ECO:0000303|PubMed:18602030};
DE Short=NDK II {ECO:0000250|UniProtKB:Q02254, ECO:0000303|PubMed:18602030};
DE Short=NDP kinase II {ECO:0000250|UniProtKB:Q02254, ECO:0000303|PubMed:18602030};
DE Short=NDPK II {ECO:0000250|UniProtKB:Q02254, ECO:0000303|PubMed:18602030};
DE Flags: Fragments;
OS Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC Pseudotsuga.
OX NCBI_TaxID=3357;
RN [1] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT "A proteomics approach to identify proteins differentially expressed in
RT Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL J. Proteomics 71:425-438(2008).
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. {ECO:0000305}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10030, ECO:0000305};
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:0000255|PROSITE-ProRule:PRU10030, ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P15531};
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000255}.
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DR AlphaFoldDB; P85930; -.
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:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR SUPFAM; SSF54919; SSF54919; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Phosphoprotein; Transferase.
FT CHAIN <1..>27
FT /note="Nucleoside diphosphate kinase 2"
FT /id="PRO_0000397960"
FT BINDING 3
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15531"
FT NON_CONS 18..19
FT /evidence="ECO:0000303|PubMed:18602030"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:18602030"
FT NON_TER 27
FT /evidence="ECO:0000303|PubMed:18602030"
SQ SEQUENCE 27 AA; 2913 MW; 96447E3575961299 CRC64;
MIKPDGVQRG LVGEIISRGD FAIDIGR
