NDK2_SPIOL
ID NDK2_SPIOL Reviewed; 233 AA.
AC Q01402;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Nucleoside diphosphate kinase 2, chloroplastic;
DE EC=2.7.4.6;
DE AltName: Full=Nucleoside diphosphate kinase II;
DE Short=NDK II;
DE Short=NDP kinase II;
DE Short=NDPK II;
DE Contains:
DE RecName: Full=Nucleoside diphosphate kinase 2 high molecular weight;
DE Contains:
DE RecName: Full=Nucleoside diphosphate kinase 2 low molecular weight;
DE Flags: Precursor;
GN Name=NDPK2;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Leaf;
RX PubMed=8381027; DOI=10.1016/0167-4781(93)90070-t;
RA Zhang J., Nomura T., Yatsunami K., Honda A., Sugimoto Y., Moriwaki T.,
RA Yamamoto J., Ohta M., Fukui T., Ichikawa A.;
RT "Nucleotide sequence of the cDNA encoding nucleoside diphosphate kinase II
RT from spinach leaves.";
RL Biochim. Biophys. Acta 1171:304-306(1993).
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.
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: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; D11465; BAA02018.1; -; mRNA.
DR PIR; S28226; S28226.
DR AlphaFoldDB; Q01402; -.
DR SMR; Q01402; -.
DR PRIDE; Q01402; -.
DR GO; GO:0009507; C:chloroplast; 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:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
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 ATP-binding; Chloroplast; Direct protein sequencing; Kinase; Magnesium;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW Plastid; Transferase; Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..233
FT /note="Nucleoside diphosphate kinase 2 high molecular
FT weight"
FT /id="PRO_0000019439"
FT CHAIN 81..233
FT /note="Nucleoside diphosphate kinase 2 low molecular
FT weight"
FT /id="PRO_0000019440"
FT ACT_SITE 199
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 233 AA; 26107 MW; F4173840F71DFEBD CRC64;
MEAMSGLSSP CNCISSLPHS SSTTTRHQNL LFRRNNHHQQ KLAAFHSQSH LFSTKCPLIS
HSLPRKKSFK PHIFLPHLVA SMEQVEETYI MIKPDGVQRG LVGEIISRFE KKGFKLIGLK
MYPCPKELAE EHYKDLKAKS FYQKLIDYIT SGPVVCMAWE GVGVVASSRK LIGATDPLQA
EPGTIRGDLA VQTGRNVVHG SDSPDNGKRE IGLWFKEGEI CQWTPAQAPW LRE
