NDK3_SPIOL
ID NDK3_SPIOL Reviewed; 153 AA.
AC P81766;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Nucleoside diphosphate kinase 3;
DE EC=2.7.4.6;
DE AltName: Full=Nucleoside diphosphate kinase III;
DE Short=NDK III;
DE Short=NDP kinase III;
DE Short=NDPK III;
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 PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC TISSUE=Leaf;
RX PubMed=7711053; DOI=10.1016/0167-4838(94)00222-3;
RA Zhang J., Fukui T., Ichikawa A.;
RT "A third type of nucleoside diphosphate kinase from spinach leaves:
RT purification, characterization and amino-acid sequence.";
RL Biochim. Biophys. Acta 1248:19-26(1995).
RN [2]
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION.
RX PubMed=14736920; DOI=10.1073/pnas.0308164100;
RA Spetea C., Hundal T., Lundin B., Heddad M., Adamska I., Andersson B.;
RT "Multiple evidence for nucleotide metabolism in the chloroplast thylakoid
RT lumen.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1409-1414(2004).
RN [3]
RP PROTEIN SEQUENCE OF 1-19, AND SUBCELLULAR LOCATION.
RX PubMed=8645740; DOI=10.1016/0167-4838(96)00032-5;
RA Yang L.M., Lamppa G.K.;
RT "Rapid purification of a chloroplast nucleoside diphosphate kinase using
RT CoA-affinity chromatography.";
RL Biochim. Biophys. Acta 1294:99-102(1996).
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. Shows the highest specificity towards GDP.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.4 uM for GDP;
CC KM=89.05 uM for ADP;
CC pH dependence:
CC Optimum pH is 6.0.;
CC -!- SUBUNIT: Homohexamer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:14736920, ECO:0000269|PubMed:8645740}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
CC -!- CAUTION: There are likely two genes coding for two slightly different
CC proteins, NDK3 and NDK4. The characterization was made on a thylakoid
CC lumen preparation containing probably both proteins. {ECO:0000305}.
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DR PIR; S60363; S60363.
DR AlphaFoldDB; P81766; -.
DR SMR; P81766; -.
DR IntAct; P81766; 1.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; 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; Thylakoid; Transferase.
FT CHAIN 1..153
FT /note="Nucleoside diphosphate kinase 3"
FT /id="PRO_0000137146"
FT ACT_SITE 117
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 153 AA; 17118 MW; E496E7D51C2B9511 CRC64;
AEFERTFIAI KPDGVQRGLI SEIVARFERK GFSLVAIKVV IPSRPFAQKH YADLKDKPFY
VGLVAYWSSG PVVAMVWEGE GVIKYGRKLI GATDPQKSEP GTIRGDLAVV NGRNIIHGSD
GPETAKDEIK LWFKPEELVN YTHNAEKWIY GDN
