NDK_ENCCU
ID NDK_ENCCU Reviewed; 147 AA.
AC Q8SRM7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Nucleoside diphosphate kinase;
DE Short=NDK;
DE Short=NDP kinase;
DE Short=NDPK;
DE EC=2.7.4.6;
GN Name=NDK1; OrderedLocusNames=ECU06_1530;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
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 -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; AL590446; CAD25514.1; -; Genomic_DNA.
DR RefSeq; NP_585910.1; NM_001041532.1.
DR PDB; 3MPD; X-ray; 2.08 A; A/B=1-147.
DR PDBsum; 3MPD; -.
DR AlphaFoldDB; Q8SRM7; -.
DR SMR; Q8SRM7; -.
DR STRING; 284813.Q8SRM7; -.
DR GeneID; 859337; -.
DR KEGG; ecu:ECU06_1530; -.
DR VEuPathDB; MicrosporidiaDB:ECU06_1530; -.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; Q8SRM7; -.
DR OMA; ALWFGEQ; -.
DR OrthoDB; 1334716at2759; -.
DR Proteomes; UP000000819; Chromosome VI.
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; Kinase; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..147
FT /note="Nucleoside diphosphate kinase"
FT /id="PRO_0000379474"
FT ACT_SITE 115
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3MPD"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:3MPD"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:3MPD"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:3MPD"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:3MPD"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3MPD"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:3MPD"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:3MPD"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:3MPD"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3MPD"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:3MPD"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3MPD"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:3MPD"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:3MPD"
SQ SEQUENCE 147 AA; 16660 MW; A358FAB807A311C8 CRC64;
MERTFIMIKP DAIKRRLISR IIQRFEEKGL YLAASKCVIP KREVLETHYS HLSSMPFFSE
MVEDMMSGMV LAMVWVGKDA VSIGRKLIGE TNPQAASVGT IRGDYGVSTG KNIIHGSDCV
ENAEKEIKLW IGDDVQPVSF FDKEWIY
