ID   NDK2_PEA                Reviewed;         230 AA.
AC   P47923;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 65-76 AND 78-107.
RC   STRAIN=cv. Golf; TISSUE=Leaf;
RX   PubMed=7580854; DOI=10.1007/bf01106759;
RA   Luebeck J., Soll J.;
RT   "Nucleoside diphosphate kinase from pea chloroplasts: purification, cDNA
RT   cloning and import into chloroplasts.";
RL   Planta 196:668-673(1995).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z37990; CAA86071.1; -; mRNA.
DR   PIR; S52785; S52785.
DR   AlphaFoldDB; P47923; -.
DR   SMR; P47923; -.
DR   BRENDA; 2.7.4.6; 4872.
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..64
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:7580854"
FT   CHAIN           65..230
FT                   /note="Nucleoside diphosphate kinase 2 high molecular
FT                   weight"
FT                   /id="PRO_0000019437"
FT   CHAIN           78..230
FT                   /note="Nucleoside diphosphate kinase 2 low molecular
FT                   weight"
FT                   /id="PRO_0000019438"
FT   ACT_SITE        196
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   230 AA;  25617 MW;  A5A10604D9E6D505 CRC64;
     MEAMAVFSGS NLFATSSLLL TTNSKTRYSQ LRTTQNLSAF SSKSHLFSPS STSSSYPKTF
     RTRSSTESGI FLPRLITSLE QVDQAYIMVK PDGVQRGLVG EIISRFEKKG FKLTGLKLFQ
     CSKELAEEHY KHLNQKSFFP KLIEYITSGP VVSMAWEGVG VVPSARKLIG ATDPLQAEPG
     TIRGDFAVQT GRNIIHGSDS PENGEREIAL WFKEGELCEW TPVQEPWLRE