ID NDK_PELPD Reviewed; 137 AA. AC A1AU17; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 89. 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}; OrderedLocusNames=Ppro_3244; OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales; OC Desulfuromonadaceae; Pelobacter. OX NCBI_TaxID=338966; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1; 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 Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D., RA Richardson P.; RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."; RL Submitted (OCT-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; CC Evidence={ECO:0000255|HAMAP-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; CP000482; ABL00838.1; -; Genomic_DNA. DR RefSeq; WP_011737055.1; NC_008609.1. DR AlphaFoldDB; A1AU17; -. DR SMR; A1AU17; -. DR STRING; 338966.Ppro_3244; -. DR KEGG; ppd:Ppro_3244; -. DR eggNOG; COG0105; Bacteria. DR HOGENOM; CLU_060216_8_1_7; -. DR OrthoDB; 9801161at2; -. DR Proteomes; UP000006732; Chromosome. 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; KW Reference proteome; Transferase. FT CHAIN 1..137 FT /note="Nucleoside diphosphate kinase" FT /id="PRO_1000026267" FT ACT_SITE 115 FT /note="Pros-phosphohistidine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 9 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 57 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 85 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 112 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" SQ SEQUENCE 137 AA; 15229 MW; 80B8C78FC879BD67 CRC64; MERTFAIIKP DAVERRLAGT VIDRIEANGF TIVGMKKIKL SKEQAGGFYC VHRERPFFGE LCDFMSRSPV IVLCLEKENA IADWRKLMGA TNPANAEPGT IRRDFALSLS ENSAHGSDAP ETAAFEIAYF FNALELV //