ID A0A0N1DTG3_9FLAO Unreviewed; 288 AA.
AC A0A0N1DTG3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:KPH11740.1};
GN Synonyms=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
GN ORFNames=AMQ68_20430 {ECO:0000313|EMBL:KPH11740.1};
OS Chryseobacterium sp. ERMR1:04.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1705393 {ECO:0000313|EMBL:KPH11740.1, ECO:0000313|Proteomes:UP000037945};
RN [1] {ECO:0000313|EMBL:KPH11740.1, ECO:0000313|Proteomes:UP000037945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:04 {ECO:0000313|EMBL:KPH11740.1,
RC ECO:0000313|Proteomes:UP000037945};
RX PubMed=26543128;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Genome Assembly of Chryseobacterium polytrichastri ERMR1:04, a
RT Psychrotolerant Bacterium with Cold Active Proteases, Isolated from East
RT Rathong Glacier in India.";
RL Genome Announc. 3:e01305-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000037945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:04 {ECO:0000313|Proteomes:UP000037945};
RA Swarnkar M.K., Kumar R., Singh A.K., Singh D.;
RT "Genome Sequencing of Chryseobacterium sp. ERMR1:04 isolated from Glacier
RT Moraine Ridge soil.";
RL Submitted (AUG-2015) 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:KPH11740.1}.
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DR EMBL; LIRF01000008; KPH11740.1; -; Genomic_DNA.
DR RefSeq; WP_054512431.1; NZ_LIRF01000008.1.
DR AlphaFoldDB; A0A0N1DTG3; -.
DR STRING; 1705393.AMQ68_20430; -.
DR PATRIC; fig|1705393.3.peg.4297; -.
DR OrthoDB; 9774737at2; -.
DR Proteomes; UP000037945; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00361}.
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 71..72
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 143..144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 184..189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ SEQUENCE 288 AA; 32576 MW; 8952155099A2C9AE CRC64;
MKAAIYSQKK DLDTFLYLSK FVSELESRGV KSVLYEVMAE ALQFSKIFET FNNKQDLIDK
EVDLFFTFGG DGTIVNSLTF IEDLEIPIVG VNTGRLGFLA SFTKEEAFKE LDAILKGDVK
TSRRAVIEVV SPRSDEFFPY ALNDVTISRK ETTSMVTVDS YINDEFLNVF WGDGVIVSTP
TGSTAYSLSC GGPIISPNNE NFVITPIAPH NLNVRPLVVN DRVEIKFKVE SRVPQYSLSL
DSRLIHIETD KEIIIKKASF QILLVQPNDL SFYETIRQKL LWGRDKRN
//
