ID NDK_THEEB Reviewed; 150 AA.
AC Q8DM56;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 66.
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=tlr0267;
OS Thermosynechococcus elongatus (strain BP-1).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
RA Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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 -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the NDK family.
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DR EMBL; BA000039; BAC07820.1; -; Genomic_DNA.
DR RefSeq; NP_681058.1; NC_004113.1.
DR ProteinModelPortal; Q8DM56; -.
DR SMR; Q8DM56; 1-149.
DR STRING; 197221.tlr0267; -.
DR EnsemblBacteria; BAC07820; BAC07820; BAC07820.
DR GeneID; 1012468; -.
DR KEGG; tel:tlr0267; -.
DR PATRIC; 23925742; VBITheElo119873_0280.
DR eggNOG; COG0105; -.
DR HOGENOM; HOG000224564; -.
DR KO; K00940; -.
DR OMA; IARFERK; -.
DR ProtClustDB; PRK00668; -.
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; Reference proteome; Transferase.
FT CHAIN 1 150 Nucleoside diphosphate kinase.
FT /FTId=PRO_0000137061.
FT ACT_SITE 115 115 Pros-phosphohistidine intermediate (By
FT similarity).
FT BINDING 9 9 ATP (By similarity).
FT BINDING 57 57 ATP (By similarity).
FT BINDING 85 85 ATP (By similarity).
FT BINDING 91 91 ATP (By similarity).
FT BINDING 102 102 ATP (By similarity).
FT BINDING 112 112 ATP (By similarity).
SQ SEQUENCE 150 AA; 16820 MW; 19FCBE3267C3B032 CRC64;
MERTFLAIKP DGVQRGLVGT IIQRFEQKGY TLVGLKLMRV SRELAEQHYG EHKDKPFFPG
LVNFITSGPV VAMVWEGRGV IANARKLIGA TNPLNAEPGT LRGDFAVDVG RNVIHGSDSP
ENAEREINLW FQTQELVPWE PALTSWVYEM
//
