ID A0A0Q8CNU7_9MICO Unreviewed; 139 AA.
AC A0A0Q8CNU7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|RuleBase:RU004013};
DE EC=2.7.4.6 {ECO:0000256|RuleBase:RU004013};
GN ORFNames=ASD61_03370 {ECO:0000313|EMBL:KRA11165.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA11165.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA11165.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11165.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA11165.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11165.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRA11165.1}.
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DR EMBL; LMGR01000001; KRA11165.1; -; Genomic_DNA.
DR RefSeq; WP_055818350.1; NZ_LMGR01000001.1.
DR AlphaFoldDB; A0A0Q8CNU7; -.
DR STRING; 1736567.ASD61_03370; -.
DR Proteomes; UP000051073; 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:KRA11165.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004013};
KW Reference proteome {ECO:0000313|Proteomes:UP000051073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004013}.
FT DOMAIN 4..139
FT /note="Nucleoside diphosphate kinase-like"
FT /evidence="ECO:0000259|SMART:SM00562"
SQ SEQUENCE 139 AA; 15172 MW; F3C50C549EEE2528 CRC64;
MTTIEETLVL VKPDGVARGL TGEILRRIEA KGYSLVDLRL VEADRDLLAQ HYAEHEGKPF
YEPLLEFMES GPSVAIRVAG NRVIEGFRSL AGTTDPTTAA PGTIRGDLGR DWGLKVQQNL
VHGSDSPESA ARELALWFA
//
