NDK4_SPIOL
ID NDK4_SPIOL Reviewed; 235 AA.
AC Q8RXA8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Nucleoside diphosphate kinase 4, chloroplastic;
DE EC=2.7.4.6;
DE AltName: Full=Nucleoside diphosphate kinase III;
DE AltName: Full=Nucleoside diphosphate kinase IV;
DE Short=NDK IV;
DE Short=NDP kinase IV;
DE Short=NDPK IV;
DE Flags: Precursor;
GN Name=NDK4; Synonyms=NDPKIII;
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].
RA Zhang J., Hu Y.;
RT "Spinach mRNA for nucleoside diphosphate kinase III.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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).
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 (By
CC 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 -!- 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}.
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 EMBL; AY082428; AAL91136.1; -; mRNA.
DR AlphaFoldDB; Q8RXA8; -.
DR SMR; Q8RXA8; -.
DR PRIDE; Q8RXA8; -.
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; Kinase; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Phosphoprotein; Plastid;
KW Thylakoid; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT TRANSIT ?..82
FT /note="Thylakoid"
FT CHAIN 83..235
FT /note="Nucleoside diphosphate kinase 4, chloroplastic"
FT /id="PRO_0000019441"
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 235 AA; 25685 MW; AB60AC38AAB977D5 CRC64;
MRSQIYRSAT KAARSFLSSS KNASSRFLPE GRTVAATAAV SLRVKAPYLA SFGGANASGT
WMSTALAIPA AAYLLQDQEA CAAEFERTFI AIKPDGVQRG LISEIVARFE RKGFKLVAIK
VVIPSKDFAQ KHYHDLSERP FFNGLCDFLS SGPVVAMVWE GEGVIKYGRK LIGATDPQKS
EPGTIRGDLA VVVGRNIIHG SDGPETAKDE IKLWFKPEEL VNYTHNAEKW IYGDN
