NDK_PYRAE
ID NDK_PYRAE Reviewed; 183 AA.
AC Q8ZWY4;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=PAE1561;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10030};
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|PROSITE-ProRule:PRU10030};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL63565.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009441; AAL63565.1; ALT_INIT; Genomic_DNA.
DR PDB; 1XQI; X-ray; 2.50 A; A/B/C=1-183.
DR PDBsum; 1XQI; -.
DR AlphaFoldDB; Q8ZWY4; -.
DR SMR; Q8ZWY4; -.
DR STRING; 178306.PAE1561; -.
DR EnsemblBacteria; AAL63565; AAL63565; PAE1561.
DR KEGG; pai:PAE1561; -.
DR PATRIC; fig|178306.9.peg.1155; -.
DR eggNOG; arCOG04313; Archaea.
DR HOGENOM; CLU_060216_6_3_2; -.
DR InParanoid; Q8ZWY4; -.
DR OMA; KIVAMKM; -.
DR BRENDA; 2.7.4.6; 5239.
DR EvolutionaryTrace; Q8ZWY4; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.141; -; 1.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR Pfam; PF00334; NDK; 2.
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..183
FT /note="Nucleoside diphosphate kinase"
FT /id="PRO_0000137097"
FT REGION 56..88
FT /note="Insert"
FT ACT_SITE 160
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10030"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:1XQI"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 55..72
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:1XQI"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:1XQI"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:1XQI"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1XQI"
SQ SEQUENCE 183 AA; 20322 MW; CFEC6F1DD9EC93FC CRC64;
MPVEKTLLIL KPDAVARGLV GEIISRFEKA GLKIVALKMV KASPEEIERF YPSSEEWLRS
AGQKLLKAYQ ELGIDPRAKI GTDDPVEVGR IIKRSLVKYM TSGPIVVMVL KGNRAVEIVR
KLVGPTSPHS APPGTIRGDY SIDSPDLAAE EGRVVFNLVH ASDSPSEAER EIRFWFREEE
VLE
