ID F4FXU2_METCR Unreviewed; 132 AA. AC F4FXU2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 03-MAY-2023, entry version 50. 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 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|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 --------------------------------------------------------------------------- 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 AlphaFoldDB; F4FXU2; -. DR STRING; 1006006.Mcup_0029; -. DR EnsemblBacteria; AEB94140; AEB94140; Mcup_0029. DR KEGG; mcn:Mcup_0029; -. DR PATRIC; fig|1006006.8.peg.29; -. DR eggNOG; arCOG04313; Archaea. DR HOGENOM; CLU_060216_6_3_2; -. DR OMA; KIVAMKM; -. DR Proteomes; UP000007812; 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|HAMAP-Rule:MF_00451, KW ECO:0000256|RuleBase:RU004013}; KW 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|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 1..132 FT /note="Nucleoside diphosphate kinase-like" FT /evidence="ECO:0000259|SMART:SM00562" FT ACT_SITE 109 FT /note="Pros-phosphohistidine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 3 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 79 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 85 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 96 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 106 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="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 //