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Database: UniProt/TrEMBL
Entry: G0HJT4_THES4
LinkDB: G0HJT4_THES4
Original site: G0HJT4_THES4 
ID   G0HJT4_THES4            Unreviewed;       174 AA.
AC   G0HJT4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   19-FEB-2014, entry version 18.
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=GQS_00215;
OS   Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=1042877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5172 / 4557;
RX   PubMed=21914870; DOI=10.1128/JB.05851-11;
RA   Wang X., Gao Z., Xu X., Ruan L.;
RT   "Complete Genome Sequence of Thermococcus sp. Strain 4557, a
RT   Hyperthermophilic Archaeon Isolated from a Deep-Sea Hydrothermal Vent
RT   Area.";
RL   J. Bacteriol. 193:5544-5545(2011).
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   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NDK family.
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DR   EMBL; CP002920; AEK71946.1; -; Genomic_DNA.
DR   RefSeq; YP_004761623.1; NC_015865.1.
DR   EnsemblBacteria; AEK71946; AEK71946; GQS_00215.
DR   GeneID; 11014691; -.
DR   KEGG; the:GQS_00215; -.
DR   KO; K00940; -.
DR   OMA; CKAADWF; -.
DR   BioCyc; TSP1042877:GHEX-42-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:UniProtKB-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   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; SSF54919; 1.
DR   PROSITE; PS00469; NDP_KINASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Endonuclease; Hydrolase;
KW   Kinase; Magnesium; Metal-binding; Nuclease; Nucleotide metabolism;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   ACT_SITE    123    123       Pros-phosphohistidine intermediate (By
FT                                similarity).
FT   BINDING      14     14       ATP (By similarity).
FT   BINDING      62     62       ATP (By similarity).
FT   BINDING      90     90       ATP (By similarity).
FT   BINDING      96     96       ATP (By similarity).
FT   BINDING     107    107       ATP (By similarity).
SQ   SEQUENCE   174 AA;  20151 MW;  A13564C4649237CC CRC64;
     MVEKKIERTL VILKPDAVVR GLMGEIISRF EKRGLKIVGM KMIWIDREMA EKHYEEHKGK
     PFFEPLIDYI TKAPSVVMVV EGRYAISVVR KMSGATDPKD AEPGSIRGDY GLDIGDSIYN
     IIHASDSPES AEREINLYFK PDELYRYCKA ADWFYHTHAR AKREYLDTMD CLER
//
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