ID NDK_HELMI Reviewed; 149 AA.
AC B0TBN6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 01-MAY-2013, entry version 39.
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=Helmi_12500; ORFNames=HM1_0677;
OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Heliobacteriaceae;
OC Heliobacterium.
OX NCBI_TaxID=498761;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51547 / Ice1;
RX PubMed=18441057; DOI=10.1128/JB.00299-08;
RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L.,
RA Wang Z.T., Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT "The genome of Heliobacterium modesticaldum, a phototrophic
RT representative of the Firmicutes containing the simplest
RT photosynthetic apparatus.";
RL J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ83875.1; -; Genomic_DNA.
DR RefSeq; YP_001679886.1; NC_010337.2.
DR ProteinModelPortal; B0TBN6; -.
DR SMR; B0TBN6; 1-149.
DR STRING; 498761.HM1_0677; -.
DR EnsemblBacteria; ABZ83875; ABZ83875; HM1_0677.
DR GeneID; 5910345; -.
DR KEGG; hmo:HM1_0677; -.
DR PATRIC; 22106759; VBIHelMod36755_1159.
DR eggNOG; COG0105; -.
DR HOGENOM; HOG000224564; -.
DR KO; K00940; -.
DR OMA; FRVVAMK; -.
DR BioCyc; HMOD498761:GI46-655-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 CHAIN 1 149 Nucleoside diphosphate kinase.
FT /FTId=PRO_1000192263.
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 149 AA; 16683 MW; 6E6E16045191E5C1 CRC64;
MERTYLMIKP DGVQRGLVGE IISRFEKKGF KLVGMKFLRL TREMAEKHYA EHVGKPFFAG
LVDYIISGPV VAMCWEGKDI VSVSREMMGA TNPAKAAPGT IRGTYAVDIG RNIIHGSDSP
ASAERELAIY FQSDELVEWD RTLQGWLTE
//
