NDK2_TOBAC
ID NDK2_TOBAC Reviewed; 232 AA.
AC Q852S5; P82855;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Flags: Precursor;
GN Name=NDPK2 {ECO:0000250|UniProtKB:O64903};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC55280.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun NN {ECO:0000269|Ref.1};
RA Yamamoto Y., Mitoh C.;
RT "NDPK from aluminum-tolerant cultured tobacco cells.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC55280.1}
RP PROTEIN SEQUENCE OF 80-89.
RC STRAIN=cv. Samsun;
RA Yamamoto Y., Asakura Y., Yamada H., Matsumoto H.;
RL Submitted (OCT-2000) to UniProtKB.
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: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:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08879};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000255}.
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DR EMBL; AB088360; BAC55280.1; -; mRNA.
DR RefSeq; NP_001311894.1; NM_001324965.1.
DR RefSeq; XP_016442628.1; XM_016587142.1.
DR AlphaFoldDB; Q852S5; -.
DR SMR; Q852S5; -.
DR STRING; 4097.Q852S5; -.
DR GeneID; 107768038; -.
DR KEGG; nta:107768038; -.
DR OMA; ITEFAFF; -.
DR OrthoDB; 1334716at2759; -.
DR Proteomes; UP000084051; Unplaced.
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; 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: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; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 80..232
FT /note="Nucleoside diphosphate kinase 2, chloroplastic"
FT /id="PRO_0000257978"
FT ACT_SITE 198
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P08879"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08879"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08879"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08879"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08879"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08879"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08879"
SQ SEQUENCE 232 AA; 25342 MW; 1AE99FD93B6CBB5E CRC64;
MGCLSVVGAS PCVSSSALSS PTSRLSCAPS CKLILNPIKK NHHLAAFQPA VHLFASNQSR
SHASKRNHTT RIFLPHLVAS MEEVEETYIM IKPDGVQRGL VGEIISRFEK KGFKLTGLKL
FHCPKELAEE HYKDLQSKPF FPKLIDYITS GPVVCMAWEG VGVVASARKL IGATNPLNAE
PGTIRGDLAV QTGRNVVHGS DSPDNGKREI ALWFGEGELC SWTPVQEPWL IE
