ID D7DAC8_STAHD Unreviewed; 141 AA. AC D7DAC8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAR-2024, entry version 59. DE RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004013}; DE Short=NDK {ECO:0000256|HAMAP-Rule:MF_00451}; DE Short=NDP kinase {ECO:0000256|HAMAP-Rule:MF_00451}; DE EC=2.7.4.6 {ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004013}; DE AltName: Full=Nucleoside-2-P kinase {ECO:0000256|HAMAP-Rule:MF_00451}; GN Name=ndk {ECO:0000256|HAMAP-Rule:MF_00451}; GN OrderedLocusNames=Shell_1639 {ECO:0000313|EMBL:ADI32724.1}; OS Staphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 / OS P8). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Staphylothermus. OX NCBI_TaxID=591019 {ECO:0000313|EMBL:ADI32724.1, ECO:0000313|Proteomes:UP000002573}; RN [1] {ECO:0000313|Proteomes:UP000002573} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8 RC {ECO:0000313|Proteomes:UP000002573}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Anderson I.J., Woyke T.; RT "Complete sequence of Staphylothermus hellenicus DSM 12710."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADI32724.1, ECO:0000313|Proteomes:UP000002573} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8 RC {ECO:0000313|Proteomes:UP000002573}; RX PubMed=22180806; DOI=10.4056/sigs.2054696; RA Anderson I., Wirth R., Lucas S., Copeland A., Lapidus A., Cheng J.F., RA Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Pati A., Mikhailova N., Woyke T., Klenk H.P., RA Kyrpides N., Ivanova N.; RT "Complete genome sequence of Staphylothermus hellenicus P8."; RL Stand. Genomic Sci. 5:12-20(2011). 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:0000256|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:0000256|HAMAP- CC Rule:MF_00451, ECO:0000256|RuleBase:RU004013}; 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:0000256|HAMAP-Rule:MF_00451}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP- CC Rule:MF_00451}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451}. CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|ARBA:ARBA00008142, CC ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004011}. 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; CP002051; ADI32724.1; -; Genomic_DNA. DR RefSeq; WP_013143921.1; NC_014205.1. DR AlphaFoldDB; D7DAC8; -. DR STRING; 591019.Shell_1639; -. DR GeneID; 9234932; -. DR KEGG; shc:Shell_1639; -. DR eggNOG; arCOG04313; Archaea. DR HOGENOM; CLU_060216_6_3_2; -. DR OrthoDB; 6874at2157; -. DR Proteomes; UP000002573; 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; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1. DR PANTHER; PTHR11349:SF91; NUCLEOSIDE DIPHOSPHATE KINASE; 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; NDP_KINASES; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00451}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004013}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00451}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00451}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00451}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00451}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00451}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00451}. FT DOMAIN 3..140 FT /note="Nucleoside diphosphate kinase-like" FT /evidence="ECO:0000259|SMART:SM00562" FT ACT_SITE 117 FT /note="Pros-phosphohistidine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 59 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 87 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 93 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 104 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" SQ SEQUENCE 141 AA; 15834 MW; 3B6CF06DFD08D8C5 CRC64; MSIERTLVLI KPDGVRRGLI GEIISRFERK GLKIKALKML WLTRDKAEEF YSVHRGKPFF ESLIEFMTSG PIIAMVLEGD MAISVVRKMI GPTDGREAPP GTIRGDYSLS KSQNVVHASD SPESAVREIG VIFKDDEIID W //