NDK_BORBU
ID NDK_BORBU Reviewed; 167 AA.
AC O51419;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 124.
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=BB_0463;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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 (By similarity). {ECO:0000250}.
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;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC66829.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000783; AAC66829.1; ALT_INIT; Genomic_DNA.
DR PIR; F70157; F70157.
DR RefSeq; NP_212597.1; NC_001318.1.
DR PDB; 4DI6; X-ray; 2.40 A; A/B/C/D/E/F=1-167.
DR PDB; 4DZ6; X-ray; 2.20 A; A/B/C/D/E/F=1-167.
DR PDBsum; 4DI6; -.
DR PDBsum; 4DZ6; -.
DR AlphaFoldDB; O51419; -.
DR SMR; O51419; -.
DR STRING; 224326.BB_0463; -.
DR PRIDE; O51419; -.
DR EnsemblBacteria; AAC66829; AAC66829; BB_0463.
DR KEGG; bbu:BB_0463; -.
DR PATRIC; fig|224326.49.peg.856; -.
DR HOGENOM; CLU_060216_6_3_12; -.
DR OMA; KIVAMKM; -.
DR BRENDA; 2.7.4.6; 902.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; 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-EC.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.141; -; 1.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00562; NDK; 1.
DR SUPFAM; SSF54919; SSF54919; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..167
FT /note="Nucleoside diphosphate kinase"
FT /id="PRO_0000136951"
FT ACT_SITE 132
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:4DZ6"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4DZ6"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:4DZ6"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4DZ6"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:4DZ6"
SQ SEQUENCE 167 AA; 19159 MW; 4A8E142C253182B8 CRC64;
MLLQKTLCIV KPDGVRRGLI GDVVSRFERV GLKMVAAKML IVDESLAKKH YLYDDIVFRH
SEAVWNSLIK FISNSPVFTF VVEGVESIEV VRKLCGATEP KLAIPGTIRG DFSYHSFKYS
NEKGFSIYNV IHASANEADA MREIPIWFKD NEILNYKRDD ECEHYYC
