NDK_CAMJE
ID NDK_CAMJE Reviewed; 137 AA.
AC Q9PIG7; Q0PBH7;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=Cj0332c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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}.
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DR EMBL; AL111168; CAL34483.1; -; Genomic_DNA.
DR PIR; H81452; H81452.
DR RefSeq; WP_002858685.1; NC_002163.1.
DR RefSeq; YP_002343770.1; NC_002163.1.
DR PDB; 3PJ9; X-ray; 2.10 A; A/B/C/D=1-137.
DR PDBsum; 3PJ9; -.
DR AlphaFoldDB; Q9PIG7; -.
DR SMR; Q9PIG7; -.
DR IntAct; Q9PIG7; 46.
DR STRING; 192222.Cj0332c; -.
DR PaxDb; Q9PIG7; -.
DR PRIDE; Q9PIG7; -.
DR EnsemblBacteria; CAL34483; CAL34483; Cj0332c.
DR GeneID; 904656; -.
DR KEGG; cje:Cj0332c; -.
DR PATRIC; fig|192222.6.peg.324; -.
DR eggNOG; COG0105; Bacteria.
DR HOGENOM; CLU_060216_8_1_7; -.
DR OMA; KIVAMKM; -.
DR BRENDA; 2.7.4.6; 13746.
DR EvolutionaryTrace; Q9PIG7; -.
DR Proteomes; UP000000799; 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:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
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 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..137
FT /note="Nucleoside diphosphate kinase"
FT /id="PRO_0000136960"
FT ACT_SITE 115
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT BINDING 9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00451"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3PJ9"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:3PJ9"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:3PJ9"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3PJ9"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:3PJ9"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:3PJ9"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3PJ9"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:3PJ9"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:3PJ9"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:3PJ9"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3PJ9"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:3PJ9"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3PJ9"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3PJ9"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:3PJ9"
SQ SEQUENCE 137 AA; 15142 MW; 53EDA6F707B45C32 CRC64;
MEKTLSIIKP DAVKKGVIGK ILDRFESNGL RIAAMKKVQL SKEQAENFYA VHKERPFFKD
LVEFMISGPV VVSILEGEGA VLKNRDLMGA TNPKEAKAGT IRADFAESID ANAVHGSDSL
ENAKIEIEFF FKPNEIC
