ID F4FXU2_METCR Unreviewed; 132 AA. AC F4FXU2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 29-APR-2015, entry version 24. 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=Mcup_0029 {ECO:0000313|EMBL:AEB94140.1}; OS Metallosphaera cuprina (strain Ar-4). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Metallosphaera. OX NCBI_TaxID=1006006 {ECO:0000313|EMBL:AEB94140.1, ECO:0000313|Proteomes:UP000007812}; RN [1] {ECO:0000313|EMBL:AEB94140.1, ECO:0000313|Proteomes:UP000007812} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ar-4 {ECO:0000313|EMBL:AEB94140.1, RC ECO:0000313|Proteomes:UP000007812}; RX PubMed=21551305; DOI=10.1128/JB.05038-11; RA Liu L.J., You X.Y., Zheng H., Wang S., Jiang C.Y., Liu S.J.; RT "Complete genome sequence of Metallosphaera cuprina, a metal sulfide- RT oxidizing archaeon from a hot spring."; RL J. Bacteriol. 193:3387-3388(2011). 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: ATP + nucleoside diphosphate = ADP + CC nucleoside triphosphate. {ECO:0000256|HAMAP-Rule:MF_00451, CC ECO:0000256|RuleBase:RU004013}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={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|HAMAP- CC 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; CP002656; AEB94140.1; -; Genomic_DNA. DR RefSeq; YP_004408624.1; NC_015435.1. DR EnsemblBacteria; AEB94140; AEB94140; Mcup_0029. DR GeneID; 10492226; -. DR KEGG; mcn:Mcup_0029; -. DR KO; K00940; -. DR OMA; PFYEPLV; -. DR BioCyc; MCUP1006006:GHTI-30-MONOMER; -. DR Proteomes; UP000007812; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.141; -; 1. DR HAMAP; MF_00451; NDP_kinase; 1. 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:UP000007812}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00451, KW 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|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 ACT_SITE 109 109 Pros-phosphohistidine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 3 3 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 51 51 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 79 79 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 85 85 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 96 96 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. FT BINDING 106 106 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}. SQ SEQUENCE 132 AA; 14602 MW; E2A78D57B6DE5F4B CRC64; MIKPDGVKRR LVGEIVARIE RKGLNIVSMK MVKIDRNTAE KLYEEHKGKS FFNELVSYIT SGPVVCMVIE GDEAVKVMRT LIGSTDPKEA SPGTIRGDLA MSKGENVIHA SDAEEKAKKE MSLFFSQNEL TG //