ID A0A951P7M4_9CYAN Unreviewed; 149 AA. AC A0A951P7M4; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 27-NOV-2024, entry version 6. 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 ECO:0000313|EMBL:MBW4464512.1}; GN ORFNames=KME07_03605 {ECO:0000313|EMBL:MBW4464512.1}; OS Pegethrix bostrychoides GSE-TBD4-15B. OC Bacteria; Cyanobacteriota; Cyanophyceae; Oculatellales; Oculatellaceae; OC Pegethrix. OX NCBI_TaxID=2839662 {ECO:0000313|EMBL:MBW4464512.1, ECO:0000313|Proteomes:UP000707356}; RN [1] {ECO:0000313|EMBL:MBW4464512.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GSE-TBD4-15B {ECO:0000313|EMBL:MBW4464512.1}; RA Pietrasiak N., Ward R., Stajich J.E., Kurbessoian T.; RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:MBW4464512.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GSE-TBD4-15B {ECO:0000313|EMBL:MBW4464512.1}; RX PubMed=34080906; RA Ward R.D., Stajich J.E., Johansen J.R., Huntemann M., Clum A., Foster B., RA Foster B., Roux S., Palaniappan K., Varghese N., Mukherjee S., RA Reddy T.B.K., Daum C., Copeland A., Chen I.A., Ivanova N.N., Kyrpides N.C., RA Shapiro N., Eloe-Fadrosh E.A., Pietrasiak N.; RT "Metagenome Sequencing to Explore Phylogenomics of Terrestrial RT Cyanobacteria."; RL Microbiol. Resour. Announc. 10:0-0(2022). CC -!- FUNCTION: (Microbial infection) Catalyzes the phosphorylation of dZDP CC to dZTP, when the bacterium is infected by a phage that produces the CC substrate for the synthesis of dZTP (2- amino-2'-deoxyadenosine 5'- CC triphosphate), which is then used by the phage as a DNA polymerase CC substrate. {ECO:0000256|ARBA:ARBA00024802}. 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=dZDP + ATP = dZTP + ADP; Xref=Rhea:RHEA:67644, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:172929, ChEBI:CHEBI:172931, CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024506}; 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|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-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|ARBA:ARBA00008142, CC ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004011}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBW4464512.1}. 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; JAHHHV010000014; MBW4464512.1; -; Genomic_DNA. DR Proteomes; UP000707356; Unassembled WGS sequence. 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 FunFam; 3.30.70.141:FF:000002; 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 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00451}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00451}; 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|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00451}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00451}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00451}. FT DOMAIN 1..138 FT /note="Nucleoside diphosphate kinase-like" FT /evidence="ECO:0000259|SMART:SM00562" FT ACT_SITE 115 FT /note="Pros-phosphohistidine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 9 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 57 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 91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" FT BINDING 112 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451" SQ SEQUENCE 149 AA; 16618 MW; 07D626830EC2FEF8 CRC64; MERTFIAIKP DGVQRQIIGE IIRRFESKGF TLVGLKIMQV SRELAEQHYA VHKERPFFPG LVNFIISAPL VAMVWEGEGV IASARKLIGA TNPLTAEPGT IRGDFGVSVG RNLIHGSDAP ETAAEEIKLW FKDEELVSWQ PASTPWLYE //