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Nucleoside diphosphate kinase (NDK) (NDP kinase) (EC 2.7.4.6) (Nucleoside-2-P kinase)

 A0A0J9WWU3_XANOP        Unreviewed;       141 AA.
A0A0J9WWU3;
14-OCT-2015, integrated into UniProtKB/TrEMBL.
14-OCT-2015, sequence version 1.
22-NOV-2017, entry version 15.
RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004013};
Short=NDK {ECO:0000256|HAMAP-Rule:MF_00451};
Short=NDP kinase {ECO:0000256|HAMAP-Rule:MF_00451};
EC=2.7.4.6 {ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004013};
AltName: Full=Nucleoside-2-P kinase {ECO:0000256|HAMAP-Rule:MF_00451};
Name=ndk {ECO:0000256|HAMAP-Rule:MF_00451};
OrderedLocusNames=PXO_01052 {ECO:0000313|EMBL:ACD59114.1},
PXO_06114 {ECO:0000313|EMBL:ACD59305.1};
Xanthomonas oryzae pv. oryzae (strain PXO99A).
Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
Xanthomonadaceae; Xanthomonas.
NCBI_TaxID=360094 {ECO:0000313|EMBL:ACD59114.1, ECO:0000313|Proteomes:UP000001740};
[1] {ECO:0000313|EMBL:ACD59114.1, ECO:0000313|Proteomes:UP000001740}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PXO99A {ECO:0000313|EMBL:ACD59114.1,
ECO:0000313|Proteomes:UP000001740};
PubMed=18452608; DOI=10.1186/1471-2164-9-204;
Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M.,
Rabinowicz P.D., Tsuge S., Furutani A., Ochiai H., Delcher A.L.,
Kelley D., Madupu R., Puiu D., Radune D., Shumway M., Trapnell C.,
Aparna G., Jha G., Pandey A., Patil P.B., Ishihara H., Meyer D.F.,
Szurek B., Verdier V., Koebnik R., Dow J.M., Ryan R.P., Hirata H.,
Tsuyumu S., Won Lee S., Seo Y.S., Sriariyanum M., Ronald P.C.,
Sonti R.V., Van Sluys M.A., Leach J.E., White F.F., Bogdanove A.J.;
"Genome sequence and rapid evolution of the rice pathogen Xanthomonas
oryzae pv. oryzae PXO99A.";
BMC Genomics 9:204-204(2008).
[2] {ECO:0000313|EMBL:ACD59114.1}
NUCLEOTIDE SEQUENCE.
STRAIN=PXO99A {ECO:0000313|EMBL:ACD59114.1};
Salzberg S.;
Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:ACD59114.1}
NUCLEOTIDE SEQUENCE.
STRAIN=PXO99A {ECO:0000313|EMBL:ACD59114.1};
Booher N.J., Carpenter S.C.D., Sebra R.P., Wang L., Salzberg S.L.,
Leach J.E., Bogdanove A.J.;
Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Major role in the synthesis of nucleoside triphosphates
other than ATP. The ATP gamma phosphate is transferred to the NDP
beta phosphate via a ping-pong mechanism, using a phosphorylated
active-site intermediate. {ECO:0000256|HAMAP-Rule:MF_00451}.
-!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
nucleoside triphosphate. {ECO:0000256|HAMAP-Rule:MF_00451,
ECO:0000256|RuleBase:RU004013}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00451};
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00451}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451}.
-!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|HAMAP-
Rule:MF_00451, ECO:0000256|RuleBase:RU004011}.
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EMBL; CP000967; ACD59114.1; -; Genomic_DNA.
EMBL; CP000967; ACD59305.1; -; Genomic_DNA.
RefSeq; WP_002812972.1; NC_010717.2.
ProteinModelPortal; A0A0J9WWU3; -.
SMR; A0A0J9WWU3; -.
EnsemblBacteria; ACD59114; ACD59114; PXO_01052.
EnsemblBacteria; ACD59305; ACD59305; PXO_06114.
GeneID; 34206990; -.
KEGG; xop:PXO_01052; -.
KEGG; xop:PXO_06114; -.
KO; K00940; -.
OMA; KIVAMKM; -.
Proteomes; UP000001740; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0006241; P:CTP biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0006183; P:GTP biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0006228; P:UTP biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 3.30.70.141; -; 2.
HAMAP; MF_00451; NDP_kinase; 1.
InterPro; IPR034907; NDK-like_dom.
InterPro; IPR036850; NDK-like_dom_sf.
InterPro; IPR001564; Nucleoside_diP_kinase.
InterPro; IPR023005; Nucleoside_diP_kinase_AS.
Pfam; PF00334; NDK; 1.
PRINTS; PR01243; NUCDPKINASE.
SMART; SM00562; NDK; 1.
SUPFAM; SSF54919; SSF54919; 1.
PROSITE; PS00469; NDP_KINASES; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00451,
ECO:0000256|RuleBase:RU004013};
Complete proteome {ECO:0000313|Proteomes:UP000001740};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451};
Kinase {ECO:0000256|HAMAP-Rule:MF_00451,
ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:ACD59114.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00451};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00451};
Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00451};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00451,
ECO:0000256|RuleBase:RU004013};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00451};
Transferase {ECO:0000256|HAMAP-Rule:MF_00451,
ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:ACD59114.1}.
DOMAIN 4 137 NDK. {ECO:0000259|Pfam:PF00334}.
ACT_SITE 117 117 Pros-phosphohistidine intermediate.
{ECO:0000256|HAMAP-Rule:MF_00451}.
BINDING 11 11 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
BINDING 59 59 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
BINDING 87 87 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
BINDING 93 93 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
BINDING 104 104 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
BINDING 114 114 ATP. {ECO:0000256|HAMAP-Rule:MF_00451}.
SEQUENCE 141 AA; 15257 MW; AB1B422F1C9D7DAF CRC64;
MALERTLSII KPDAVAKNVI GEIYSRFEKA GLKVVAAKYK QLSRREAEGF YAVHRERPFF
NALVEFMISG PVMIQALEGE NAVAAHRDLL GATNPKDAAP GTIRADFADS IDANAAHGSD
SVENAANEVA YFFAATEVVS R


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