ID A0A0F7HL61_9STAP Unreviewed; 268 AA.
AC A0A0F7HL61;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361};
DE EC=2.7.1.23 {ECO:0000256|HAMAP-Rule:MF_00361};
DE AltName: Full=ATP-dependent NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361};
GN Name=ppnK {ECO:0000313|EMBL:AKG74259.1};
GN Synonyms=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
GN ORFNames=AAT16_08445 {ECO:0000313|EMBL:AKG74259.1}, SAMN05216235_2584
GN {ECO:0000313|EMBL:SFK93649.1};
OS Salinicoccus halodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX NCBI_TaxID=407035 {ECO:0000313|EMBL:AKG74259.1, ECO:0000313|Proteomes:UP000034029};
RN [1] {ECO:0000313|EMBL:AKG74259.1, ECO:0000313|Proteomes:UP000034029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3B36 {ECO:0000313|EMBL:AKG74259.1,
RC ECO:0000313|Proteomes:UP000034029};
RX PubMed=26634017;
RA Jiang K., Xue Y., Ma Y.;
RT "Complete genome sequence of Salinicoccus halodurans H3B36, isolated from
RT the Qaidam Basin in China.";
RL Stand. Genomic Sci. 10:116-116(2015).
RN [2] {ECO:0000313|Proteomes:UP000034029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3B36 {ECO:0000313|Proteomes:UP000034029};
RA Ma Y., Jiang K., Xue Y.;
RT "Complete genome sequence of Salinicoccus halodurans strain H3B36, isolated
RT from the Qaidam basin of China.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFK93649.1, ECO:0000313|Proteomes:UP000183090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6501 {ECO:0000313|EMBL:SFK93649.1,
RC ECO:0000313|Proteomes:UP000183090};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the regulation of the intracellular balance of
CC NAD and NADP, and is a key enzyme in the biosynthesis of NADP.
CC Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
CC adenosine moiety of NAD to yield NADP. {ECO:0000256|HAMAP-
CC Rule:MF_00361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001262, ECO:0000256|HAMAP-
CC Rule:MF_00361};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00361};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00361}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00361}.
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DR EMBL; CP011366; AKG74259.1; -; Genomic_DNA.
DR EMBL; FOTB01000006; SFK93649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7HL61; -.
DR STRING; 407035.AAT16_08445; -.
DR KEGG; shv:AAT16_08445; -.
DR PATRIC; fig|407035.3.peg.1747; -.
DR OrthoDB; 9774737at2; -.
DR Proteomes; UP000034029; Chromosome.
DR Proteomes; UP000183090; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProt.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_00361; NAD_kinase; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002504; NADK.
DR PANTHER; PTHR20275; NAD KINASE; 1.
DR PANTHER; PTHR20275:SF9; NAD KINASE 2; 1.
DR Pfam; PF20143; NAD_kinase_C; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00361};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00361};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00361};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00361};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00361};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00361}.
FT ACT_SITE 53
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 53..54
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 125..126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 165..170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ SEQUENCE 268 AA; 30526 MW; 7D78B70C4EBC8345 CRC64;
MNNNIYKTVY FFAPHGEETK EVHDELSDLF ARHGIEEVQS SDDAEIIASI GGDGEFLQSV
RKNNFRDDCV YLGIAVDESN YFYVDFHYRD IKTLEEAIDQ DNLDVRNYPL LEVSINDNKP
SYCLNEFTLR SSIVKTIKMD VYINDFLFEQ FNGDGILVAT PTGSTGYNKS LGGSVVDPLI
HAMQVTELAS VNNNTHRTLG TSFLLNKDRP LTLLIDKNVD YYPIMSLDND ALSVRNTEKI
EVGISDKLIK TLKLKDNTFW HKAQRNFL
//
