ID A0A4V2NMC2_9GAMM Unreviewed; 253 AA.
AC A0A4V2NMC2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 21.
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=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
GN ORFNames=EZM97_04975 {ECO:0000313|EMBL:TCI12697.1};
OS Dyella soli.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Lysobacterales; Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=522319 {ECO:0000313|EMBL:TCI12697.1, ECO:0000313|Proteomes:UP000291822};
RN [1] {ECO:0000313|EMBL:TCI12697.1, ECO:0000313|Proteomes:UP000291822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 12747 {ECO:0000313|EMBL:TCI12697.1,
RC ECO:0000313|Proteomes:UP000291822};
RA Gao Z.-H., Qiu L.-H.;
RT "Dyella amyloliquefaciens sp. nov., isolated from forest soil.";
RL Submitted (FEB-2019) 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=NAD(+) + ATP = ADP + NADP(+) + H(+); 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:ARBA00047925, 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:TCI12697.1}.
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DR EMBL; SJTG01000001; TCI12697.1; -; Genomic_DNA.
DR RefSeq; WP_131150522.1; NZ_SJTG01000001.1.
DR AlphaFoldDB; A0A4V2NMC2; -.
DR Proteomes; UP000291822; 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:UniProtKB-ARBA.
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 Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR Gene3D; 2.60.200.30; Probable inorganic polyphosphate/atp-NAD kinase, domain 2; 1.
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 NCBIfam; NF003406; PRK04761.1; 1.
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:UP000291822};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00361}.
FT ACT_SITE 41
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 41..42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 111..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 152..157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ SEQUENCE 253 AA; 28071 MW; CCD1852C9128D71A CRC64;
MAYSFVASDT SIAQQARKKL VERYGEVSPE QAEAIVALGG DGFMLRTLHA YRSLGVPVYG
MKLGRVGFLM NKHRIDDLPR RIERAHTASL FPLEMQVTDA SGHMHEALAF NEVSLLRQSN
QAAHLEVKLN EAVKLESLVC DGILVSTPAG STAYNLSAHG PILPLDANVL ALTPISPFRP
RRWRGAILPH RTQVTLRVID PGKRPVSATA DFHEVRDVKE VTVRQSEGPA VRLLFDPEHN
LEQRILDEQF AQD
//
