ID A0A0A7V2I4_9ARCH Unreviewed; 339 AA.
AC A0A0A7V2I4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=A7X95_01835 {ECO:0000313|EMBL:PTL88037.1}, T478_0793
GN {ECO:0000313|EMBL:AJA93063.1};
OS Candidatus Nitrosopelagicus brevis.
OC Archaea; Nitrososphaerota.
OX NCBI_TaxID=1410606 {ECO:0000313|EMBL:AJA93063.1, ECO:0000313|Proteomes:UP000030944};
RN [1] {ECO:0000313|EMBL:AJA93063.1, ECO:0000313|Proteomes:UP000030944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN25 {ECO:0000313|EMBL:AJA93063.1}, and V2
RC {ECO:0000313|Proteomes:UP000030944};
RX PubMed=25587132; DOI=10.1073/pnas.1416223112;
RA Santoro A.E., Dupont C.L., Richter R.A., Craig M.T., Carini P.,
RA McIlvin M.R., Yang Y., Orsi W.D., Moran D.M., Saito M.A.;
RT "Genomic and proteomic characterization of "Candidatus Nitrosopelagicus
RT brevis": An ammonia-oxidizing archaeon from the open ocean.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:1173-1178(2015).
RN [2] {ECO:0000313|EMBL:PTL88037.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U25 {ECO:0000313|EMBL:PTL88037.1};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000241022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U25 {ECO:0000313|Proteomes:UP000241022};
RA Dupont C., Santoro A.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PTL88037.1, ECO:0000313|Proteomes:UP000241022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U25 {ECO:0000313|EMBL:PTL88037.1,
RC ECO:0000313|Proteomes:UP000241022};
RA Carini P.;
RT "Transcriptomics of ammonia oxidizing archaea.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-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; CP007026; AJA93063.1; -; Genomic_DNA.
DR EMBL; LXWN01000001; PTL88037.1; -; Genomic_DNA.
DR RefSeq; WP_048105391.1; NZ_LXWN01000001.1.
DR STRING; 1410606.T478_0793; -.
DR GeneID; 24816684; -.
DR KEGG; nbv:T478_0793; -.
DR HOGENOM; CLU_008831_0_2_2; -.
DR OrthoDB; 350804at2157; -.
DR Proteomes; UP000030944; Chromosome.
DR Proteomes; UP000241022; Unassembled WGS sequence.
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: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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:UP000030944};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00361}.
FT ACT_SITE 50
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 121..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
FT BINDING 162..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361"
SQ SEQUENCE 339 AA; 37652 MW; 6D98A664AD793F12 CRC64;
MHVGIFGTGL TDSSERILKK ILDENHISSS KIGTKSKNKK SDCVFVLGGD KGVRNYFHRT
FDASIPVLGI NESESDGFLS QLDLKQLPSL ISRIKKMDFE TEQVTRLGVK IDGKNVYPVL
NDVAVFSSRS AMLMEHTLRV NGDEVWHDSS DGIIISTPIG SSAYSMSAGG PVIFQDSDVF
GIISVNSIDI TRRPLVVSNA SVIEVDEISS RLHCEVVLDG LDRYKVKNSV EATNYEPSAN
IIRLKKDTTA ISAIAKKVKL AEELFNMPPS SKLLLKILEY EGSMSQKELV KKTMLPDRTV
RLAMSHLLEK GYVKKKVSIR DSRQKIYEIS KLINSDLQQ
//
