ID A0A4Q8N2B9_9STAP Unreviewed; 159 AA. AC A0A4Q8N2B9; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 18-SEP-2019, entry version 2. 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 ORFNames=DMB77_04250 {ECO:0000313|EMBL:TAA94724.1}; OS Staphylococcus saccharolyticus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=33028 {ECO:0000313|EMBL:TAA94724.1, ECO:0000313|Proteomes:UP000293857}; RN [1] {ECO:0000313|EMBL:TAA94724.1, ECO:0000313|Proteomes:UP000293857} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DVP4-17-2404 {ECO:0000313|EMBL:TAA94724.1, RC ECO:0000313|Proteomes:UP000293857}; RA Bruggemann H., Poehlein A., Brzuszkiewicz E., Scavenius C., RA Enghild J.J., Al-Zeer M.A., Brinkmann V., Jensen A., Soderquist B.; RT "Staphylococcus saccharolyticus isolated from blood cultures and RT prosthetic joint infections exhibits excessive genome decay."; RL Submitted (MAY-2018) 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: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 CC 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; CC EC=2.7.4.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00451}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00451}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00451}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451}. CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|HAMAP- CC Rule:MF_00451, ECO:0000256|RuleBase:RU004011}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:TAA94724.1}. 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; QHKC01000001; TAA94724.1; -; Genomic_DNA. DR Proteomes; UP000293857; Unassembled WGS sequence. 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00451, KW ECO:0000256|RuleBase:RU004013}; KW Complete proteome {ECO:0000313|Proteomes:UP000293857}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00451, KW ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:TAA94724.1}; 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|HAMAP-Rule:MF_00451, KW ECO:0000256|RuleBase:RU004013}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00451}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00451, KW ECO:0000256|RuleBase:RU004013}. FT DOMAIN 11 148 NDK. {ECO:0000259|SMART:SM00562}. FT ACT_SITE 125 125 Pros-phosphohistidine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 19 19 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 67 67 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 95 95 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 101 101 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 112 112 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 122 122 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. SQ SEQUENCE 159 AA; 17772 MW; 39C86292527D95C2 CRC64; MKHTHRGTHI VERTFLIIKP DAVQRNLIGE IVTRIEKKGL KLVGGKLMQV PKELAEKHYS EHEGKPFYDK LISFITSAPV FAMVVEGENA VAVSRHIIGS TNPSEAAPGT IRGDLGLTLG RNIIHGSDSV ESAQREVKLW FNSNEIADYL APREDWLYE //