(data stored in SCRATCH3701 zone)

SWISSPROT: NDK_RICTY

ID   NDK_RICTY               Reviewed;         140 AA.
AC   Q68XS9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=Nucleoside diphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00451};
DE            Short=NDK {ECO:0000255|HAMAP-Rule:MF_00451};
DE            Short=NDP kinase {ECO:0000255|HAMAP-Rule:MF_00451};
DE            EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_00451};
DE   AltName: Full=Nucleoside-2-P kinase {ECO:0000255|HAMAP-Rule:MF_00451};
GN   Name=ndk {ECO:0000255|HAMAP-Rule:MF_00451}; OrderedLocusNames=RT0077;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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:0000255|HAMAP-Rule:MF_00451}.
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:0000255|HAMAP-
CC         Rule:MF_00451};
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:0000255|HAMAP-Rule:MF_00451};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00451};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00451}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00451}.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000255|HAMAP-
CC       Rule:MF_00451}.
DR   EMBL; AE017197; AAU03563.1; -; Genomic_DNA.
DR   RefSeq; WP_011190550.1; NC_006142.1.
DR   SMR; Q68XS9; -.
DR   STRING; 257363.RT0077; -.
DR   EnsemblBacteria; AAU03563; AAU03563; RT0077.
DR   KEGG; rty:RT0077; -.
DR   eggNOG; ENOG4108UGX; Bacteria.
DR   eggNOG; COG0105; LUCA.
DR   HOGENOM; HOG000224565; -.
DR   KO; K00940; -.
DR   OMA; KIVAMKM; -.
DR   OrthoDB; 1752581at2; -.
DR   BioCyc; RTYP257363:G1G0L-78-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
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:0006228; P:UTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.141; -; 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   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;
DR   PRODOM; Q68XS9.
DR   SWISS-2DPAGE; Q68XS9.
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN           1..140
FT                   /note="Nucleoside diphosphate kinase"
FT                   /id="PRO_0000137036"
FT   ACT_SITE        117
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         11
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         59
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         87
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         93
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         104
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT   BINDING         114
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
SQ   SEQUENCE   140 AA;  15831 MW;  4DFF101A3DF76D6E CRC64;
     MTIQYTFSMI KPDVIKRNKI GQVNTYLENA GLKIVAQKMK FLTKYEAECF YDEHRARPFF
     NSLVEYITSG AVVLQVLKGE DAITLNRIIM GATNPAEAKE GTIRKDLGES IEANSIHGSD
     SENSAKREIK FFFSKSEIIE
//

If you have problems or comments...

PBIL Back to PBIL home page