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Database: UniProt
Entry: A0A062VIL5_9MICO
LinkDB: A0A062VIL5_9MICO
Original site: A0A062VIL5_9MICO 
ID   A0A062VIL5_9MICO        Unreviewed;       138 AA.
AC   A0A062VIL5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|RuleBase:RU004013};
DE            EC=2.7.4.6 {ECO:0000256|RuleBase:RU004013};
GN   ORFNames=DC31_10400 {ECO:0000313|EMBL:KDA06262.1};
OS   Microbacterium sp. CH12i.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA06262.1, ECO:0000313|Proteomes:UP000027096};
RN   [1] {ECO:0000313|EMBL:KDA06262.1, ECO:0000313|Proteomes:UP000027096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH12i {ECO:0000313|EMBL:KDA06262.1,
RC   ECO:0000313|Proteomes:UP000027096};
RA   Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.;
RT   "Draft genome sequence of Microbacterium sp. strain CH12i, isolated from
RT   shallow groundwater in Cape Hallet, Antarctica.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|RuleBase:RU004013};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|ARBA:ARBA00008142,
CC       ECO:0000256|RuleBase:RU004011}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDA06262.1}.
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DR   EMBL; JHET01000004; KDA06262.1; -; Genomic_DNA.
DR   RefSeq; WP_036277917.1; NZ_JHET01000004.1.
DR   AlphaFoldDB; A0A062VIL5; -.
DR   STRING; 1479651.DC31_10400; -.
DR   OrthoDB; 9801161at2; -.
DR   Proteomes; UP000027096; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   CDD; cd04413; NDPk_I; 1.
DR   Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 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   PANTHER; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR   PANTHER; PTHR11349:SF91; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1.
DR   PROSITE; PS00469; NDP_KINASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004013};
KW   Kinase {ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:KDA06262.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027096};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004013}.
FT   DOMAIN          3..138
FT                   /note="Nucleoside diphosphate kinase-like"
FT                   /evidence="ECO:0000259|SMART:SM00562"
SQ   SEQUENCE   138 AA;  14876 MW;  4C27020A65240A2F CRC64;
     MATEETLVLV KPDGVARGLT GAILARIEAK GYALVDIRLV EPDRDVLAEH YAEHEGKPFY
     EPLLEFMMSG PAVAIRLTGN RVIEGFRSLA GTTDPTTAAP GTIRGDFGRD WGLAVQQNLV
     HGSDSPESAA RELGIWFA
//
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