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 05-JUL-2017, entry version 70. 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=Ppro_3244; OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1). OC Bacteria; Proteobacteria; Deltaproteobacteria; 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., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Lovley D., 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 CC other than ATP. The ATP gamma phosphate is transferred to the NDP CC beta phosphate via a ping-pong mechanism, using a phosphorylated CC active-site intermediate. {ECO:0000255|HAMAP-Rule:MF_00451}. CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP + CC nucleoside triphosphate. {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 ProteinModelPortal; A1AU17; -. DR SMR; A1AU17; -. DR STRING; 338966.Ppro_3244; -. DR EnsemblBacteria; ABL00838; ABL00838; Ppro_3244. DR KEGG; ppd:Ppro_3244; -. DR eggNOG; ENOG4108UGX; Bacteria. DR eggNOG; COG0105; LUCA. DR HOGENOM; HOG000224565; -. DR KO; K00940; -. DR OMA; KIVAMKM; -. DR OrthoDB; POG091H040S; -. DR Proteomes; UP000006732; Chromosome. DR GO; GO:0005737; C:cytoplasm; 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: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; 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1 137 Nucleoside diphosphate kinase. FT /FTId=PRO_1000026267. FT ACT_SITE 115 115 Pros-phosphohistidine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 9 9 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 57 57 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 85 85 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 91 91 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 102 102 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 112 112 ATP. {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 //