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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
 
 
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