ID F4FXU2_METCR Unreviewed; 132 AA. AC F4FXU2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 06-MAR-2013, entry version 10. DE RecName: Full=Nucleoside diphosphate kinase; DE Short=NDK; DE Short=NDP kinase; DE EC=2.7.4.6; DE AltName: Full=Nucleoside-2-P kinase; GN Name=ndk; OrderedLocusNames=Mcup_0029; OS Metallosphaera cuprina (strain Ar-4). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Metallosphaera. OX NCBI_TaxID=1006006; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ar-4; 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 (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP + CC nucleoside triphosphate. CC -!- COFACTOR: Magnesium (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the NDK family. 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 GeneID; 10492226; -. DR KEGG; mcn:Mcup_0029; -. DR KO; K00940; -. DR OMA; FRVVAMK; -. DR BioCyc; MCUP1006006:GHTI-29-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:HAMAP. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:HAMAP. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:HAMAP. DR GO; GO:0006228; P:UTP biosynthetic process; IEA: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 PANTHER; PTHR11349; PTHR11349; 1. DR Pfam; PF00334; NDK; 1. DR PRINTS; PR01243; NUCDPKINASE. DR SMART; SM00562; NDK; 1. DR SUPFAM; SSF54919; NDK; 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; Transferase. FT ACT_SITE 109 109 Pros-phosphohistidine intermediate (By FT similarity). FT BINDING 3 3 ATP (By similarity). FT BINDING 51 51 ATP (By similarity). FT BINDING 79 79 ATP (By similarity). FT BINDING 85 85 ATP (By similarity). FT BINDING 96 96 ATP (By similarity). FT BINDING 106 106 ATP (By similarity). SQ SEQUENCE 132 AA; 14602 MW; E2A78D57B6DE5F4B CRC64; MIKPDGVKRR LVGEIVARIE RKGLNIVSMK MVKIDRNTAE KLYEEHKGKS FFNELVSYIT SGPVVCMVIE GDEAVKVMRT LIGSTDPKEA SPGTIRGDLA MSKGENVIHA SDAEEKAKKE MSLFFSQNEL TG //