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Database: UniProt
Entry: A0A0E3ZCC1_9BACT
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ID   A0A0E3ZCC1_9BACT        Unreviewed;       295 AA.
AC   A0A0E3ZCC1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:AKD02525.1};
GN   Synonyms=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
GN   ORFNames=PKOR_04530 {ECO:0000313|EMBL:AKD02525.1};
OS   Pontibacter korlensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD02525.1, ECO:0000313|Proteomes:UP000033109};
RN   [1] {ECO:0000313|EMBL:AKD02525.1, ECO:0000313|Proteomes:UP000033109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X14-1T {ECO:0000313|EMBL:AKD02525.1,
RC   ECO:0000313|Proteomes:UP000033109};
RX   PubMed=26057562; DOI=10.1038/srep10929;
RA   Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA   Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT   "Unraveling adaptation of Pontibacter korlensis to radiation and
RT   infertility in desert through complete genome and comparative
RT   transcriptomic analysis.";
RL   Sci. Rep. 5:10929-10929(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}.
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DR   EMBL; CP009621; AKD02525.1; -; Genomic_DNA.
DR   RefSeq; WP_046309399.1; NZ_CP009621.1.
DR   AlphaFoldDB; A0A0E3ZCC1; -.
DR   STRING; 400092.PKOR_04530; -.
DR   KEGG; pko:PKOR_04530; -.
DR   PATRIC; fig|400092.3.peg.1013; -.
DR   HOGENOM; CLU_008831_0_3_10; -.
DR   OrthoDB; 9774737at2; -.
DR   Proteomes; UP000033109; 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:UP000033109};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00361}.
FT   ACT_SITE        73
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         73..74
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         146..147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         176
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT   BINDING         187..192
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   295 AA;  32830 MW;  8C3F9B7AB8A99DF9 CRC64;
     MKIAILGKPF SDNIQPFIQT LFDELQRRKA QLCMVEHFEL YLKNTINLPT GIETFRRGDR
     LEGVDVVLSI GGDGTLLDTV TYVGEQQIPI LGINTGRLGF LATIPYDSVN IALDALYKGH
     YTLDDRALIR VDSDQEVFKG INFGLNEFSV QKRDTSSMIV VHTYIDGEYL NSYWADGLVV
     ATPTGSTGYS LSCGGPLVLP QTNNFVISPV CPHNLNVRPM IVSDRSVISF EVEGRSSSYL
     AALDSRSTPV DMNVQLAVRR EAFVARLVKL HHVNFLSTLR SKLNWGLDKR NSSIK
//
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