ID   NDK1_PEA                Reviewed;         149 AA.
AC   P47922; Q41047;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Nucleoside diphosphate kinase 1;
DE            EC=2.7.4.6;
DE   AltName: Full=Nucleoside diphosphate kinase I;
DE            Short=NDK I;
DE            Short=NDP kinase I;
DE            Short=NDPK I;
GN   Name=NDPK1; Synonyms=NDKN1;
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].
RC   STRAIN=cv. Feltham First; TISSUE=Seed;
RX   PubMed=8003697; DOI=10.1007/bf00024198;
RA   Finan P., White I.R., Redpath S.H., Findlay J.B.C., Millner P.A.;
RT   "Molecular cloning, sequence determination and heterologous expression of
RT   nucleoside diphosphate kinase from Pisum sativum.";
RL   Plant Mol. Biol. 25:59-67(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Alaska;
RX   PubMed=9868801; DOI=10.1016/s1011-1344(98)00169-9;
RA   Tanaka N., Ogura T., Noguchi T., Hirano H., Yabe N., Hasunuma K.;
RT   "Phytochrome-mediated light signals are transduced to nucleoside
RT   diphosphate kinase in Pisum sativum L. cv. Alaska.";
RL   J. Photochem. Photobiol. B 45:113-121(1998).
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. This NDK is microtubule-associated.
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   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR   EMBL; X71388; CAA50511.1; -; mRNA.
DR   EMBL; D86052; BAA12982.1; -; mRNA.
DR   PIR; S46513; S33170.
DR   AlphaFoldDB; P47922; -.
DR   SMR; P47922; -.
DR   EnsemblPlants; Psat4g223480.1; Psat4g223480.1.cds; Psat4g223480.
DR   Gramene; Psat4g223480.1; Psat4g223480.1.cds; Psat4g223480.
DR   BRENDA; 2.7.4.6; 4872.
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:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding; Phosphoprotein; Phytochrome signaling pathway;
KW   Transferase.
FT   CHAIN           1..149
FT                   /note="Nucleoside diphosphate kinase 1"
FT                   /id="PRO_0000137142"
FT   ACT_SITE        116
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        140
FT                   /note="E -> Q (in Ref. 2; BAA12982)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   149 AA;  16463 MW;  7F1E17795BE598C0 CRC64;
     MAEQTFIMIK PDGVQRGLVG EIISRFEKKG FYLKGLKFVN VERAFAEKHY ADLSAKPFFS
     GLVDYIISGP VVAMIWEGKN VVTTGRKIIG ATNPAQSEPG TIRGDFAIDI GRNVIHGSDA
     VESANKEIAL WFPEGAANWE SSLHSWIYE