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NAD kinase (EC 2.7.1.23) (ATP-dependent NAD kinase)

 A0A0A8WLV5_9DELT        Unreviewed;       285 AA.
A0A0A8WLV5;
04-MAR-2015, integrated into UniProtKB/TrEMBL.
04-MAR-2015, sequence version 1.
27-SEP-2017, entry version 20.
RecName: Full=NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00675869};
EC=2.7.1.23 {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00675836};
AltName: Full=ATP-dependent NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361};
Name=nadK {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000313|EMBL:GAM07899.1};
ORFNames=OR1_00168 {ECO:0000313|EMBL:GAM07899.1};
Geobacter sp. OR-1.
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
Geobacteraceae; Geobacter.
NCBI_TaxID=1266765 {ECO:0000313|EMBL:GAM07899.1, ECO:0000313|Proteomes:UP000030972};
[1] {ECO:0000313|EMBL:GAM07899.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM07899.1,
ECO:0000313|Proteomes:UP000030972};
PubMed=23668621; DOI=10.1021/es400231x;
Ohtsuka T., Yamaguchi N., Makino T., Sakurai K., Kimura K., Kudo K.,
Homma E., Dong DT., Amachi S.;
"Arsenic dissolution from Japanese paddy soil by a dissimilatory
arsenate-reducing bacterium Geobacter sp. OR-1.";
Environ. Sci. Technol. 47:6263-6271(2013).
[2] {ECO:0000313|EMBL:GAM07899.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM07899.1,
ECO:0000313|Proteomes:UP000030972};
Ehara A., Suzuki H., Amachi S.;
"Draft Genome Sequence of Geobacter sp. Strain OR-1, an Arsenate-
Respiring Bacterium Isolated from Japanese Paddy Soil.";
Genome Announc. 3:e01478-14(2015).
-!- FUNCTION: Involved in the regulation of the intracellular balance
of NAD and NADP, and is a key enzyme in the biosynthesis of NADP.
Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
adenosine moiety of NAD to yield NADP. {ECO:0000256|HAMAP-
Rule:MF_00361}.
-!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+).
{ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00675844}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675863};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675859}.
-!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000256|HAMAP-
Rule:MF_00361, ECO:0000256|SAAS:SAAS00675868}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00361}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:GAM07899.1}.
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EMBL; BAZF01000001; GAM07899.1; -; Genomic_DNA.
RefSeq; WP_041969370.1; NZ_BAZF01000001.1.
EnsemblBacteria; GAM07899; GAM07899; OR1_00168.
Proteomes; UP000030972; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 2.60.200.30; -; 1.
Gene3D; 3.40.50.10330; -; 1.
HAMAP; MF_00361; NAD_kinase; 1.
InterPro; IPR017438; ATP-NAD_kinase_dom_1.
InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
InterPro; IPR016064; NAD/diacylglycerol_kinase.
InterPro; IPR002504; NADK.
PANTHER; PTHR20275; PTHR20275; 1.
Pfam; PF01513; NAD_kinase; 1.
SUPFAM; SSF111331; SSF111331; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675838};
Complete proteome {ECO:0000313|Proteomes:UP000030972};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675839};
Kinase {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00638807, ECO:0000313|EMBL:GAM07899.1};
NAD {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00638803};
NADP {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00638791};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675838};
Reference proteome {ECO:0000313|Proteomes:UP000030972};
Transferase {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00638807, ECO:0000313|EMBL:GAM07899.1}.
NP_BIND 67 68 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
NP_BIND 141 142 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
NP_BIND 182 187 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
ACT_SITE 67 67 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00361}.
BINDING 152 152 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
BINDING 169 169 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
BINDING 171 171 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
BINDING 242 242 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
SEQUENCE 285 AA; 30994 MW; 0E128782161DF0D7 CRC64;
MKRVAIIAKV HDPRCQGVAG ELIEWLSAQG VEPLVEAHLA RHLLYPNGIE SARFPELADL
VVVLGGDGTL ISAARLIGGR NIPILGVNLG SLGFLTEITV PELYPMLSDC LRGKFKLSER
MMLDCTIERG GAEIACHQVL NDVVINKGAL ARIVDLDTRV DSHYLTTFKA DGLIISTPTG
STGYSLSAGG AIIHPSLNCI AITPICPHTL TNRPIVVGND SLVSIMVSSL DDEDVYLTLD
GQVGVELKSG DLIHVRRARH YSHLVMSNKR DFFEVLRTKL KWGER


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