ID A0A090ITQ9_9BACI Unreviewed; 264 AA.
AC A0A090ITQ9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=ppnK1 {ECO:0000313|EMBL:CEE01082.1};
GN Synonyms=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
GN ORFNames=B4065_2029 {ECO:0000313|EMBL:KIO67253.1}, B4167_3739
GN {ECO:0000313|EMBL:KIO71482.1}, BT1A1_1250
GN {ECO:0000313|EMBL:CEE01082.1}, CQJ30_06675
GN {ECO:0000313|EMBL:AWI11875.1};
OS Caldibacillus thermoamylovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE01082.1, ECO:0000313|Proteomes:UP000040576};
RN [1] {ECO:0000313|EMBL:CEE01082.1, ECO:0000313|Proteomes:UP000040576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg Daniel;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000032071, ECO:0000313|Proteomes:UP000032076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4065 {ECO:0000313|EMBL:KIO67253.1,
RC ECO:0000313|Proteomes:UP000032071}, and B4167
RC {ECO:0000313|EMBL:KIO71482.1, ECO:0000313|Proteomes:UP000032076};
RA Krawcyk A.O., Berendsen E.M., Eijlander R.T., de Jong A., Wells-Bennik M.,
RA Kuipers O.P.;
RT "Draft Genome Sequences of Four Bacillus thermoamylovorans Strains,
RT Isolated From Food Products.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AWI11875.1, ECO:0000313|Proteomes:UP000244914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSBM {ECO:0000313|EMBL:AWI11875.1,
RC ECO:0000313|Proteomes:UP000244914};
RX PubMed=29625286; DOI=10.1016/j.biortech.2018.03.121;
RA Cai L., Zheng S.W., Shen Y.J., Zheng G.D., Liu H.T., Wu Z.Y.;
RT "Complete genome sequence provides insights into the biodrying-related
RT microbial function of Bacillus thermoamylovorans isolated from sewage
RT sludge biodrying material.";
RL Bioresour. Technol. 260:141-149(2018).
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; CP023704; AWI11875.1; -; Genomic_DNA.
DR EMBL; CCRF01000040; CEE01082.1; -; Genomic_DNA.
DR EMBL; JXLS01000032; KIO67253.1; -; Genomic_DNA.
DR EMBL; JXLU01000127; KIO71482.1; -; Genomic_DNA.
DR RefSeq; WP_034769159.1; NZ_JXLU01000127.1.
DR AlphaFoldDB; A0A090ITQ9; -.
DR STRING; 35841.B4167_3739; -.
DR KEGG; bthv:CQJ30_06675; -.
DR PATRIC; fig|35841.6.peg.2621; -.
DR eggNOG; COG0061; Bacteria.
DR Proteomes; UP000032071; Unassembled WGS sequence.
DR Proteomes; UP000032076; Unassembled WGS sequence.
DR Proteomes; UP000040576; Unassembled WGS sequence.
DR Proteomes; UP000244914; Chromosome.
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; 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:UP000040576};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00361}.
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 45..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 122..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ SEQUENCE 264 AA; 30194 MW; 1BB6CB2A7A3D40BF CRC64;
MKFAIVSKGD EKSNTLSEKL KSYLTDFKLE YDEIEPEITI SVGGDGTLLS AFQRYRHRLN
DTAFVGIHTG HLGFYADWMP DEIEKLVIAI AKTKCRIVEY PLLEVIIYYN NERKEEHYLA
LNEATIKSVE GTFVIDVEIK DELFERFRGD GLCVSTPSGS TAYNKALGGA IIHPSLESIQ
IAEMASINNR VFRTIGSPLI LPAHHKCIFR PVTHKDFLIG IDHLTFVQKD IQSLQFRVAD
QKIRFARYKP FPFWSRVRAS FIDE
//
