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NAD kinase (EC 2.7.1.23) (ATP-dependent NAD kinase)

 Q6UCQ1_9PROT            Unreviewed;       255 AA.
Q6UCQ1;
05-JUL-2004, integrated into UniProtKB/TrEMBL.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 76.
RecName: Full=NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00675869};
EC=2.7.1.23 {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00675836};
AltName: Full=ATP-dependent NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361};
Name=nadK {ECO:0000256|HAMAP-Rule:MF_00361};
ORFNames=HOT2C01.29 {ECO:0000313|EMBL:AAR05339.1};
uncultured marine alpha proteobacterium HOT2C01.
Bacteria; Proteobacteria; Alphaproteobacteria; environmental samples.
NCBI_TaxID=248049 {ECO:0000313|EMBL:AAR05339.1};
[1] {ECO:0000313|EMBL:AAR05339.1}
NUCLEOTIDE SEQUENCE.
PubMed=14566056; DOI=10.1073/pnas.2133554100;
De La Torre J.R., Christianson L.M., Beja O., Suzuki M.T., Karl D.M.,
Heidelberg J., DeLong E.F.;
"Proteorhodopsin genes are distributed among divergent marine
bacterial taxa.";
Proc. Natl. Acad. Sci. U.S.A. 100:12830-12835(2003).
[2] {ECO:0000313|EMBL:AAR05339.1}
NUCLEOTIDE SEQUENCE.
Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the regulation of the intracellular balance
of NAD and NADP, and is a key enzyme in the biosynthesis of NADP.
Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
adenosine moiety of NAD to yield NADP. {ECO:0000256|HAMAP-
Rule:MF_00361}.
-!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+).
{ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00675844}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675863};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675859}.
-!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000256|HAMAP-
Rule:MF_00361, ECO:0000256|SAAS:SAAS00675868}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00361}.
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EMBL; AY372455; AAR05339.1; -; Genomic_DNA.
ProteinModelPortal; Q6UCQ1; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 2.60.200.30; -; 1.
Gene3D; 3.40.50.10330; -; 1.
HAMAP; MF_00361; NAD_kinase; 1.
InterPro; IPR017438; ATP-NAD_kinase_dom_1.
InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
InterPro; IPR016064; NAD/diacylglycerol_kinase.
InterPro; IPR002504; NADK.
PANTHER; PTHR20275; PTHR20275; 1.
Pfam; PF01513; NAD_kinase; 1.
SUPFAM; SSF111331; SSF111331; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675838};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675839};
Kinase {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00638807, ECO:0000313|EMBL:AAR05339.1};
NAD {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00638803};
NADP {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00638791};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00675838};
Transferase {ECO:0000256|HAMAP-Rule:MF_00361,
ECO:0000256|SAAS:SAAS00638807, ECO:0000313|EMBL:AAR05339.1}.
NP_BIND 44 45 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
NP_BIND 114 115 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
NP_BIND 155 160 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
ACT_SITE 44 44 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00361}.
BINDING 144 144 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.
SEQUENCE 255 AA; 28259 MW; C0AE2B9D873B693D CRC64;
MNLNKPVFLA SSSDEASSQK KILEDKYGNA DFDNADVIVV LGGDGFMLEA IKSHMDKHLP
IFGLNYGSVG FLMNSSNEND LINRINQSQS IKISPLIMKA KSVYGSIHEA IAINEVSLLR
ETHQASKIKI SVDGKVRLDE LICDGVLIST PSGSTAYNLS AHGPILPINA DVLALTPISA
FRPRRWKGAI LNNESNVKFE IIENEKRPVS VVADSTEFRD ISSVEVHQSK DQVVELLFDE
DHSFDERILN EQFKF


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