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Database: UniProt
Entry: A0A136I271_9ALTE
LinkDB: A0A136I271_9ALTE
Original site: A0A136I271_9ALTE 
ID   A0A136I271_9ALTE        Unreviewed;       291 AA.
AC   A0A136I271;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   03-MAY-2023, entry version 29.
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:KXJ61941.1};
GN   Synonyms=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
GN   ORFNames=AXW14_02080 {ECO:0000313|EMBL:KXJ61941.1};
OS   Alteromonas sp. Nap_26.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1795869 {ECO:0000313|EMBL:KXJ61941.1, ECO:0000313|Proteomes:UP000070342};
RN   [1] {ECO:0000313|Proteomes:UP000070342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-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:KXJ61941.1}.
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DR   EMBL; LSMP01000034; KXJ61941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136I271; -.
DR   Proteomes; UP000070342; 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         145..146
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         156
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         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         186..191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   291 AA;  31966 MW;  75D34781BA1C376C CRC64;
     MPYQTIALIG KPQHAATHDS LNILAEYLLA RGCDLLVEEN IAEELETDNF RSCNLVTIGK
     EADLAVVVGG DGSMLGAARV LARFDIHVVG VNRGNLGFLT DIHPDEITQQ LDLIFSGDCV
     VEKRFLLEVS VYRHEKLKSS NSAVNEVVLH HGKVAHMMEF EIYIDEQFVF SQRSDGLIVA
     TPTGSTAYSL SAGGPIIMPK LDALTLVPMF PHTLSSRPIV VDADSQVSMK VSKVNSDSLQ
     VSCDSHIVLP VLPGDEIRIN KSTDKLHLVH PKGYSYFNVL RKKLGWGSKL Y
//
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