NADK_ACIC5
ID NADK_ACIC5 Reviewed; 285 AA.
AC C1F1S2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361};
DE EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361};
DE AltName: Full=ATP-dependent NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361};
GN Name=nadK {ECO:0000255|HAMAP-Rule:MF_00361}; OrderedLocusNames=ACP_0680;
OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS 7670 / NBRC 15755 / NCIMB 13165 / 161).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Acidobacterium.
OX NCBI_TaxID=240015;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB
RC 13165 / 161;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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:0000255|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:0000255|HAMAP-Rule:MF_00361};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00361}.
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DR EMBL; CP001472; ACO32179.1; -; Genomic_DNA.
DR RefSeq; WP_015895856.1; NC_012483.1.
DR AlphaFoldDB; C1F1S2; -.
DR SMR; C1F1S2; -.
DR STRING; 240015.ACP_0680; -.
DR EnsemblBacteria; ACO32179; ACO32179; ACP_0680.
DR KEGG; aca:ACP_0680; -.
DR eggNOG; COG0061; Bacteria.
DR HOGENOM; CLU_008831_0_1_0; -.
DR OMA; VNLGHVG; -.
DR OrthoDB; 1463423at2; -.
DR Proteomes; UP000002207; 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 Gene3D; 2.60.200.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
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 Pfam; PF01513; NAD_kinase; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..285
FT /note="NAD kinase"
FT /id="PRO_1000133556"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 68..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 142..143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT BINDING 242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ SEQUENCE 285 AA; 30749 MW; 87EB0A5245095412 CRC64;
MRRIAVIAKP QKDELASLLP ELLAWLHGHG YDPVIDDIAA TYTSEARIVP RADLPNENPE
LVIVLGGDGT LLAAARVFAK TGVPILSVNL GSLGFLTEVP LGDLYRHLEG WAQNCCNIEQ
RAMLHCELRR DGHQVCEYEA LNDVVVSKGA IARMGDFRID LDGALVAAFR ADGVIISTPT
GSTAYSLAAN GPILAPNVDA LIVTPVCPHL LTLRPLVVQG NADLKLKVAG IPDQTYLTVD
GQEAIALCVG DEIHCRKSVY TVKLVRLGST GFFDVLRAKL KWGER
