ID NDK_ACTSZ Reviewed; 141 AA. AC A6VMK7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 02-SEP-2026, entry version 90. DE RecName: Full=Nucleoside diphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00451}; DE Short=NDK {ECO:0000255|HAMAP-Rule:MF_00451}; DE Short=NDP kinase {ECO:0000255|HAMAP-Rule:MF_00451}; DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_00451}; DE AltName: Full=Nucleoside-2-P kinase {ECO:0000255|HAMAP-Rule:MF_00451}; GN Name=ndk {ECO:0000255|HAMAP-Rule:MF_00451}; GN OrderedLocusNames=Asuc_0834; OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / OS 130Z). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=339671; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z; RX PubMed=21118570; DOI=10.1186/1471-2164-11-680; RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A., RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L., RA Burkhart K.B., Harkins V., Vieille C.; RT "A genomic perspective on the potential of Actinobacillus succinogenes for RT industrial succinate production."; RL BMC Genomics 11:680-680(2010). 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:0000255|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:0000255|HAMAP- CC Rule:MF_00451}; 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:0000255|HAMAP-Rule:MF_00451}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00451}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00451}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00451}. CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000255|HAMAP- CC Rule:MF_00451}. 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; CP000746; ABR74204.1; -; Genomic_DNA. DR RefSeq; WP_012072582.1; NC_009655.1. DR AlphaFoldDB; A6VMK7; -. DR SMR; A6VMK7; -. DR STRING; 339671.Asuc_0834; -. DR KEGG; asu:Asuc_0834; -. DR eggNOG; COG0105; Bacteria. DR HOGENOM; CLU_060216_8_1_6; -. DR OrthoDB; 9801161at2; -. DR Proteomes; UP000001114; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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:0006228; P:UTP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd04413; NDPk_I; 1. DR FunFam; 3.30.70.141:FF:000001; Nucleoside diphosphate kinase; 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 NCBIfam; NF001908; PRK00668.1; 1. DR PANTHER; PTHR46161; NUCLEOSIDE DIPHOSPHATE KINASE; 1. DR PANTHER; PTHR46161:SF3; NUCLEOSIDE DIPHOSPHATE KINASE DDB_G0292928-RELATED; 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; NDPK; 1. DR PROSITE; PS51374; NDPK_LIKE; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Nucleotide metabolism; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase. FT CHAIN 1..141 FT /note="Nucleoside diphosphate kinase" FT /id="PRO_1000072358" FT ACT_SITE 117 FT /note="Pros-phosphohistidine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 59 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 87 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 93 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 104 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" FT BINDING 114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451" SQ SEQUENCE 141 AA; 15874 MW; 3C3B233C82A6E143 CRC64; MALERTLSII KPDAVERNLV GKILSRFEEN GFQIVAMKML RLNQAQAEGF YAEHQGKPFF DGLVEYMTSA PVVVSVLEKD NAVKDYRTLI GATDPQQAAE GTIRKDFAES RRRNSVHGSD SEESAVREIA YFFVESEICP R //