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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   26-NOV-2014, entry version 25.
DE   RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00451};
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};
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:AEK71946.1};
GN   OrderedLocusNames=GQS_00215 {ECO:0000313|EMBL:AEK71946.1};
OS   Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK71946.1, ECO:0000313|Proteomes:UP000000874};
RN   [1] {ECO:0000313|EMBL:AEK71946.1, ECO:0000313|Proteomes:UP000000874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
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. {ECO:0000256|HAMAP-Rule:MF_00451}.
CC   -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC       nucleoside triphosphate. {ECO:0000256|HAMAP-Rule:MF_00451,
CC       ECO:0000256|RuleBase:RU004013}.
CC   -!- COFACTOR:
CC       Note=Magnesium. {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|HAMAP-
CC       Rule:MF_00451}.
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DR   EMBL; CP002920; AEK71946.1; -; Genomic_DNA.
DR   RefSeq; WP_014011631.1; NC_015865.1.
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; VWEGDNI; -.
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: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 {ECO:0000256|HAMAP-Rule:MF_00451,
KW   ECO:0000256|RuleBase:RU004013};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000874};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451};
KW   Endonuclease {ECO:0000313|EMBL:AEK71946.1};
KW   Hydrolase {ECO:0000313|EMBL:AEK71946.1};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00451,
KW   ECO:0000256|RuleBase:RU004013};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00451};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00451};
KW   Nuclease {ECO:0000313|EMBL:AEK71946.1};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00451};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00451,
KW   ECO:0000256|RuleBase:RU004013};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00451};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00451,
KW   ECO:0000256|RuleBase:RU004013}.
FT   ACT_SITE    123    123       Pros-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING      14     14       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING      62     62       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING      90     90       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING      96     96       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING     107    107       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
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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