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Database: UniProt
Entry: A0A0S8DJ92_9PROT
LinkDB: A0A0S8DJ92_9PROT
Original site: A0A0S8DJ92_9PROT 
ID   A0A0S8DJ92_9PROT        Unreviewed;       230 AA.
AC   A0A0S8DJ92;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   03-MAY-2023, entry version 23.
DE   SubName: Full=Inorganic polyphosphate kinase {ECO:0000313|EMBL:KPK35036.1};
DE   Flags: Fragment;
GN   ORFNames=AMJ66_02290 {ECO:0000313|EMBL:KPK35036.1};
OS   Betaproteobacteria bacterium SG8_40.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1703389 {ECO:0000313|EMBL:KPK35036.1, ECO:0000313|Proteomes:UP000051602};
RN   [1] {ECO:0000313|EMBL:KPK35036.1, ECO:0000313|Proteomes:UP000051602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_40 {ECO:0000313|EMBL:KPK35036.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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};
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:KPK35036.1}.
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DR   EMBL; LJTS01000024; KPK35036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8DJ92; -.
DR   PATRIC; fig|1703389.3.peg.1831; -.
DR   Proteomes; UP000051602; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProt.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProt.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
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   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPK35036.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   NON_TER         230
FT                   /evidence="ECO:0000313|EMBL:KPK35036.1"
SQ   SEQUENCE   230 AA;  24129 MW;  E9F237FE1AAFA3DC CRC64;
     MSLFKSVALI GKYKSPEIAE PLLKLASFLA QRGVSVKLDT LTAEHIGHND HAVASLDEIG
     ATCELAVVIG GDGTMLNIAR TFAPYDVALV GVNQGRLGFL TDLSMETMTE SIGSILDGDF
     VTESRMLLES EVVLDDKPGS KVLAFNDVSI NKGADGSLIE IEVHIDGRFV YNLRSDGLIV
     ASPTGSTAYA LSSGGPILHP GLNCIALVPV SPHTLSNRPI VVGGDSAIEI
//
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