ID A0A0F4QNX2_9GAMM Unreviewed; 143 AA.
AC A0A0F4QNX2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004013};
DE Short=NDK {ECO:0000256|HAMAP-Rule:MF_00451};
DE Short=NDP kinase {ECO:0000256|HAMAP-Rule:MF_00451};
DE EC=2.7.4.6 {ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004013};
DE AltName: Full=Nucleoside-2-P kinase {ECO:0000256|HAMAP-Rule:MF_00451};
GN Name=ndk {ECO:0000256|HAMAP-Rule:MF_00451};
GN ORFNames=AC626_20920 {ECO:0000313|EMBL:KNC65794.1}, C3B51_16455
GN {ECO:0000313|EMBL:RZM77523.1}, CWB98_09775
GN {ECO:0000313|EMBL:TMP37459.1}, CWB99_09360
GN {ECO:0000313|EMBL:TMP29393.1}, CWC22_016245
GN {ECO:0000313|EMBL:QPB84452.1}, TW77_11245
GN {ECO:0000313|EMBL:KJZ08950.1};
OS Pseudoalteromonas rubra.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ08950.1, ECO:0000313|Proteomes:UP000033452};
RN [1] {ECO:0000313|EMBL:KJZ08950.1, ECO:0000313|Proteomes:UP000033452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ08950.1,
RC ECO:0000313|Proteomes:UP000033452};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
RN [2] {ECO:0000313|Proteomes:UP000036850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OCN096 {ECO:0000313|Proteomes:UP000036850};
RA Beurmann S., Ushijima B., Belcaid M., Callahan S.M., Aeby G.S.;
RT "Draft genome sequence of a Pseudoalteromonas rubra strain, OCN096,
RT isolated from Kaneohe Bay, Oahu, Hawaii.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KNC65794.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OCN096 {ECO:0000313|EMBL:KNC65794.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:RZM77523.1, ECO:0000313|Proteomes:UP000292345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1946 {ECO:0000313|EMBL:RZM77523.1,
RC ECO:0000313|Proteomes:UP000292345};
RA Paulsen S., Gram L., Machado H.;
RT "Co-occurrence of chitin degradation, pigmentation and bioactivity in
RT marine Pseudoalteromonas.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Proteomes:UP000306719, ECO:0000313|Proteomes:UP000310249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2599 {ECO:0000313|EMBL:TMP37459.1,
RC ECO:0000313|Proteomes:UP000306719}, and S2676
RC {ECO:0000313|EMBL:TMP29393.1, ECO:0000313|Proteomes:UP000310249};
RA Paulsen S., Gram L.K.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|Proteomes:UP000306719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2599 {ECO:0000313|Proteomes:UP000306719};
RA Sonnenschein E.C., Bech P.K.;
RT "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT Pseudoalteromonas.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:TMP29393.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S2599 {ECO:0000313|EMBL:TMP37459.1}, and S2676
RC {ECO:0000313|EMBL:TMP29393.1, ECO:0000313|Proteomes:UP000310249};
RA Sonnenschein E.C., Bech P.K.;
RT "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT Pseudoalteromonas.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:QPB84452.1, ECO:0000313|Proteomes:UP000305729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4059 {ECO:0000313|EMBL:QPB84452.1,
RC ECO:0000313|Proteomes:UP000305729};
RA Paulsen S., Wang X.;
RT "Pseudoalteromonas rubra S4059.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_00451}.
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:0000256|HAMAP-
CC Rule:MF_00451, ECO:0000256|RuleBase:RU004013};
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:0000256|HAMAP-Rule:MF_00451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00451};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00451}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00451}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|ARBA:ARBA00008142,
CC ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004011}.
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DR EMBL; JXYA01000023; KJZ08950.1; -; Genomic_DNA.
DR EMBL; LFZX01000227; KNC65794.1; -; Genomic_DNA.
DR EMBL; CP045429; QPB84452.1; -; Genomic_DNA.
DR EMBL; PPUZ01000044; RZM77523.1; -; Genomic_DNA.
DR EMBL; PNCI01000018; TMP29393.1; -; Genomic_DNA.
DR EMBL; PNCJ01000014; TMP37459.1; -; Genomic_DNA.
DR RefSeq; WP_010383936.1; NZ_RHIA01000007.1.
DR AlphaFoldDB; A0A0F4QNX2; -.
DR STRING; 43658.AT705_08885; -.
DR GeneID; 61356604; -.
DR PATRIC; fig|43658.5.peg.2376; -.
DR OrthoDB; 9801161at2; -.
DR Proteomes; UP000033452; Unassembled WGS sequence.
DR Proteomes; UP000036850; Unassembled WGS sequence.
DR Proteomes; UP000292345; Unassembled WGS sequence.
DR Proteomes; UP000305729; Chromosome 1.
DR Proteomes; UP000306719; Unassembled WGS sequence.
DR Proteomes; UP000310249; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04413; NDPk_I; 1.
DR Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 1.
DR HAMAP; MF_00451; NDP_kinase; 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; PTHR46161; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR PANTHER; PTHR46161:SF3; NUCLEOSIDE DIPHOSPHATE KINASE DDB_G0292928-RELATED; 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|HAMAP-
KW Rule:MF_00451};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00451};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00451, ECO:0000256|RuleBase:RU004013};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00451};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00451};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP-
KW Rule:MF_00451};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00451,
KW ECO:0000256|RuleBase:RU004013};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00451};
KW Reference proteome {ECO:0000313|Proteomes:UP000033452};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00451}.
FT DOMAIN 3..140
FT /note="Nucleoside diphosphate kinase-like"
FT /evidence="ECO:0000259|SMART:SM00562"
FT ACT_SITE 117
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00451"
SQ SEQUENCE 143 AA; 15738 MW; 895D66928B1DE4E8 CRC64;
MALERTFSIV KPDAVAKNHI GAIYNRFESA GLKIVAAKMI HLSQEKAEGF YAEHKERPFF
GALVEFMTSG PVMVQVLEGE DAIRKNREIM GATNPAEALA GTLRADYADS IDENAVHGSD
APESAAREIA YFFTEEELCA RTR
//
