(data stored in ACNUC7421 zone)

SWISSPROT: C8W3S9_DESAS

ID   C8W3S9_DESAS            Unreviewed;       149 AA.
AC   C8W3S9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 58.
DE   RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004013};
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, ECO:0000256|RuleBase:RU004013};
DE   AltName: Full=Nucleoside-2-P kinase {ECO:0000256|HAMAP-Rule:MF_00451};
GN   Name=ndk {ECO:0000256|HAMAP-Rule:MF_00451};
GN   OrderedLocusNames=Dtox_0230 {ECO:0000313|EMBL:ACV61183.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61183.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61183.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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:
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:0000256|HAMAP-
CC         Rule:MF_00451, ECO:0000256|RuleBase:RU004013};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside
CC         5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216;
CC         EC=2.7.4.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00451};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00451};
CC   -!- SUBUNIT: Homotetramer. {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, ECO:0000256|RuleBase:RU004011}.
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DR   EMBL; CP001720; ACV61183.1; -; Genomic_DNA.
DR   RefSeq; WP_015755904.1; NC_013216.1.
DR   STRING; 485916.Dtox_0230; -.
DR   EnsemblBacteria; ACV61183; ACV61183; Dtox_0230.
DR   KEGG; dae:Dtox_0230; -.
DR   eggNOG; ENOG4108UGX; Bacteria.
DR   eggNOG; COG0105; LUCA.
DR   HOGENOM; HOG000224564; -.
DR   KO; K00940; -.
DR   OMA; KIVAMKM; -.
DR   OrthoDB; 1752581at2; -.
DR   BioCyc; DACE485916:G1GFV-235-MONOMER; -.
DR   Proteomes; UP000002217; 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; C8W3S9.
DR   SWISS-2DPAGE; C8W3S9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00451,
KW   ECO:0000256|RuleBase:RU004013};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00451,
KW   ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:ACV61183.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00451};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00451};
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   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00451,
KW   ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:ACV61183.1}.
FT   DOMAIN        1    138       NDK. {ECO:0000259|SMART:SM00562}.
FT   ACT_SITE    115    115       Pros-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING       9      9       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING      57     57       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING      85     85       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING      91     91       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING     102    102       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
FT   BINDING     112    112       ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
SQ   SEQUENCE   149 AA;  16611 MW;  2ECECE4A0A8A9CD7 CRC64;
     MERTFVMVKP DGVQRGLVAK VINSFEQKGC KLVALKMMKI DRELAEKHYG EHKGKPFFTP
     LVDYIISGPV VAMVLEGKDV ITAARNVMGA TNPLQAAIGT IRGDYGMDIG RNVVHGSDSP
     ASAQREINLF FLPEEITEWS RTLETWIFE
//

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