ID A0A164S9E3_9NOCA Unreviewed; 321 AA.
AC A0A164S9E3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:KZF12171.1};
GN Synonyms=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
GN ORFNames=A2J03_17720 {ECO:0000313|EMBL:KZF12171.1};
OS Rhodococcus sp. EPR-157.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF12171.1, ECO:0000313|Proteomes:UP000077673};
RN [1] {ECO:0000313|EMBL:KZF12171.1, ECO:0000313|Proteomes:UP000077673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR-157 {ECO:0000313|EMBL:KZF12171.1,
RC ECO:0000313|Proteomes:UP000077673};
RA Ploux O.;
RL Submitted (MAR-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}.
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:KZF12171.1}.
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DR EMBL; LVCV01000085; KZF12171.1; -; Genomic_DNA.
DR RefSeq; WP_068369673.1; NZ_LVCV01000085.1.
DR AlphaFoldDB; A0A164S9E3; -.
DR OrthoDB; 9774737at2; -.
DR Proteomes; UP000077673; 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:SF0; NAD KINASE; 1.
DR Pfam; PF01513; NAD_kinase; 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 Reference proteome {ECO:0000313|Proteomes:UP000077673};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00361}.
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 97..98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 171..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 212..217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ SEQUENCE 321 AA; 34039 MW; B0D1300AA8F4E992 CRC64;
MPVTTGVPVT SPVREVLLVS HPGRRDIAET ARRVAKVFGE AGIRLRVLLD EVDSTRIEAL
GADKTDTELA SDLTLNVIEF GPEAGVGCEL VLVLGGDGTF LRAAELAQAA GIPVLGINLG
RIGFLAEAEV DNLEDALARV ISRDYRIESR MTLDIAIRVG DQVVERGWAL NEASIENGSR
LGVLEVVLEV DGRPVSAFGC DGVLVATPTG STAYAFSAGG PVVWPELEAI LVIPSNAHAL
FARPLVTSPE SFIAVETDAG GHDALVFCDG RRTMKLPAGG RVEVIRGAAP IKWVRLDSAP
FADRMVTKFA LPTSGWRGRA R
//
