ID NDK_NITOC Reviewed; 143 AA.
AC Q3JCN5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 29-MAY-2013, entry version 52.
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=Noc_0899;
OS Nitrosococcus oceani (strain ATCC 19707 / NCIMB 11848).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Chromatiaceae; Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / NCIMB 11848;
RX PubMed=16957257; DOI=10.1128/AEM.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M.,
RA Poret-Peterson A.T., Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic,
RT ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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 -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the NDK family.
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DR EMBL; CP000127; ABA57411.1; -; Genomic_DNA.
DR RefSeq; YP_342941.1; NC_007484.1.
DR ProteinModelPortal; Q3JCN5; -.
DR SMR; Q3JCN5; 3-138.
DR STRING; 323261.Noc_0899; -.
DR EnsemblBacteria; ABA57411; ABA57411; Noc_0899.
DR GeneID; 3707226; -.
DR KEGG; noc:Noc_0899; -.
DR PATRIC; 22705666; VBINitOce57959_1072.
DR eggNOG; COG0105; -.
DR HOGENOM; HOG000224565; -.
DR KO; K00940; -.
DR OMA; AEGFYYV; -.
DR ProtClustDB; CLSK2770991; -.
DR BioCyc; NOCE323261:GCI3-908-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:HAMAP.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:HAMAP.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:HAMAP.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.30.70.141; -; 1.
DR HAMAP; MF_00451; NDP_kinase; 1; -.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR PANTHER; PTHR11349; PTHR11349; 1.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00562; NDK; 1.
DR SUPFAM; SSF54919; NDK; 1.
DR PROSITE; PS00469; NDP_KINASES; FALSE_NEG.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding;
KW Phosphoprotein; Transferase.
FT CHAIN 1 143 Nucleoside diphosphate kinase.
FT /FTId=PRO_0000226565.
FT ACT_SITE 117 117 Pros-phosphohistidine intermediate (By
FT similarity).
FT BINDING 11 11 ATP (By similarity).
FT BINDING 59 59 ATP (By similarity).
FT BINDING 87 87 ATP (By similarity).
FT BINDING 93 93 ATP (By similarity).
FT BINDING 104 104 ATP (By similarity).
FT BINDING 114 114 ATP (By similarity).
SQ SEQUENCE 143 AA; 15815 MW; 54B3C65190D46E39 CRC64;
MVIERTLSII KPDAVAKNII GEIYTRFENA GLRIVAARML HLSKEQAQEF YTVHKDRPFY
NDLVGFMTSG PVMVQVLEGE NAIARNREIM GATNPKEAVP GTIRADFAEN IDANAVHGSD
GSGTAEQEIN FFFKSEDICP RIG
//
