ID NDK_RHOP5 Reviewed; 140 AA. AC Q07LG4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Nucleoside diphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00451}; DE Short=NDK {ECO:0000255|HAMAP-Rule:MF_00451}; DE Short=NDP kinase {ECO:0000255|HAMAP-Rule:MF_00451}; DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_00451}; DE AltName: Full=Nucleoside-2-P kinase {ECO:0000255|HAMAP-Rule:MF_00451}; GN Name=ndk {ECO:0000255|HAMAP-Rule:MF_00451}; GN OrderedLocusNames=RPE_3287; OS Rhodopseudomonas palustris (strain BisA53). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=316055; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisA53; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y., RA Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisA53."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. 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:0000255|HAMAP-Rule:MF_00451}. 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:0000255|HAMAP- CC Rule:MF_00451}; 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:0000255|HAMAP-Rule:MF_00451}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00451}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00451}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00451}. CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000255|HAMAP- CC Rule:MF_00451}. 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; CP000463; ABJ07220.1; -; Genomic_DNA. DR AlphaFoldDB; Q07LG4; -. DR SMR; Q07LG4; -. DR STRING; 316055.RPE_3287; -. DR KEGG; rpe:RPE_3287; -. DR eggNOG; COG0105; Bacteria. DR HOGENOM; CLU_060216_8_1_5; -. DR OrthoDB; 9801161at2; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd04413; NDPk_I; 1. DR Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 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 PANTHER; PTHR46161; NUCLEOSIDE DIPHOSPHATE KINASE; 1. DR PANTHER; PTHR46161:SF3; NUCLEOSIDE DIPHOSPHATE KINASE DDB_G0292928-RELATED; 1. DR Pfam; PF00334; NDK; 1. DR PRINTS; PR01243; NUCDPKINASE. DR SMART; SM00562; NDK; 1. DR SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1. DR PROSITE; PS00469; NDPK; 1. DR PROSITE; PS51374; NDPK_LIKE; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Nucleotide metabolism; Nucleotide-binding; Phosphoprotein; Transferase. FT CHAIN 1..140 FT /note="Nucleoside diphosphate kinase" FT /id="PRO_1000026282" FT ACT_SITE 117 FT /note="Pros-phosphohistidine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 59 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 87 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 93 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 104 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" SQ SEQUENCE 140 AA; 15247 MW; CAF0AB2FB009D6C6 CRC64; MAVQRTFSIL KPDATERNLT GAINALIEKA GLRIVAQKRI RMTREQAETF YAVHKERPFF GELVDFMISG PVVVQVLEGE DAVLKHRDVM GATDPSKAAD GTIRKLHAKS IGENSVHGSD APETAAIEIA QFFSGNEIVG //