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Database: UniProt
Entry: B9CNZ9_9ACTN
LinkDB: B9CNZ9_9ACTN
Original site: B9CNZ9_9ACTN 
ID   B9CNZ9_9ACTN            Unreviewed;       286 AA.
AC   B9CNZ9;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   03-MAY-2023, entry version 69.
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=ATORI0001_0200 {ECO:0000313|EMBL:EEE16712.1};
OS   Lancefieldella rimae ATCC 49626.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Lancefieldella.
OX   NCBI_TaxID=553184 {ECO:0000313|EMBL:EEE16712.1, ECO:0000313|Proteomes:UP000004070};
RN   [1] {ECO:0000313|EMBL:EEE16712.1, ECO:0000313|Proteomes:UP000004070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49626 {ECO:0000313|EMBL:EEE16712.1,
RC   ECO:0000313|Proteomes:UP000004070};
RA   Madupu R., Sebastian Y., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (JAN-2009) 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:EEE16712.1}.
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DR   EMBL; ACFE01000005; EEE16712.1; -; Genomic_DNA.
DR   RefSeq; WP_003150580.1; NZ_ACFE01000005.1.
DR   AlphaFoldDB; B9CNZ9; -.
DR   STRING; 1383.IV60_GL001011; -.
DR   eggNOG; COG0061; Bacteria.
DR   Proteomes; UP000004070; 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   CDD; cd03128; GAT_1; 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   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        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         60..61
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         65
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         138..139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         239
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   286 AA;  30840 MW;  BCD5D87776AB917C CRC64;
     MKVLLVPNYS REVAVSSAHM LEEWLFDQGC DVVWAHDKKL FPHKRIDPSD CQLVISLGGD
     GTLLRAARIV GYSEIPIIGI SYGHLGFLTS ATPDEMLQTL TDALSGELHV SRRATLEIES
     VYEAPDGTQY SEKSFALNDF AVSRGGNGDM IEFSVSVSGN YIDTLRGDGF IVSTATGSTG
     YALAAGGPIV TPEFTGMSCV PIAPHTIMAR AFLTSSSDIV EITMSRERPA YCHFFADGQN
     VVHPDGAVAI CATVKRGPGD IILLDRSAQS FYRSVSRVFY GKANNS
//
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