GenomeNet

Database: UniProt
Entry: A0A0M5KTG3_9GAMM
LinkDB: A0A0M5KTG3_9GAMM
Original site: A0A0M5KTG3_9GAMM 
ID   A0A0M5KTG3_9GAMM        Unreviewed;       272 AA.
AC   A0A0M5KTG3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=W908_00250 {ECO:0000313|EMBL:ALE01173.1};
OS   Candidatus Pseudothioglobus singularis PS1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX   NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE01173.1, ECO:0000313|Proteomes:UP000068905};
RN   [1] {ECO:0000313|EMBL:ALE01173.1, ECO:0000313|Proteomes:UP000068905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS1 {ECO:0000313|EMBL:ALE01173.1,
RC   ECO:0000313|Proteomes:UP000068905};
RX   PubMed=26494659;
RA   Marshall K.T., Morris R.M.;
RT   "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT   Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL   Genome Announc. 3:e01155-e01115(2015).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006911; ALE01173.1; -; Genomic_DNA.
DR   RefSeq; WP_020023688.1; NZ_CP006911.1.
DR   AlphaFoldDB; A0A0M5KTG3; -.
DR   STRING; 1125411.W908_00250; -.
DR   KEGG; tsn:W908_00250; -.
DR   PATRIC; fig|1125411.7.peg.49; -.
DR   OrthoDB; 9774737at2; -.
DR   Proteomes; UP000068905; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000068905};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00361}.
FT   ACT_SITE        54
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         54..55
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         128..129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         139
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         158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         169..174
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   272 AA;  30060 MW;  55086E9EBF1C8D14 CRC64;
     MFNSVGVICK PNDFTSQKTA LELGVLLKDL GVNFLQDQEK FESEADLIIV VGGDGTILNT
     ARTYVDFNIP ILGVNLGRLG FLADVSVDSM ATVVSEILNG EYIKEQRALL SCQVEKNDEV
     LSQHLAFNEV VIHRNATPRM IEFELYVDDD FVNNQRADGI IITTPTGSTA YALSSGGPIM
     HPSTNAICLV SISPHTMSHR PFILHGESEV LINLLDCDER ATISFDAQSS LSASEGVALR
     IKRHSNFVHL IHPKGYDYFE IIRSKLHWGQ KV
//
DBGET integrated database retrieval system