ID   NADK_METPE              Reviewed;         270 AA.
AC   B8GEC2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Mpal_2339;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(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: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}.
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; CP001338; ACL17623.1; -; Genomic_DNA.
DR   RefSeq; WP_012618942.1; NC_011832.1.
DR   AlphaFoldDB; B8GEC2; -.
DR   SMR; B8GEC2; -.
DR   STRING; 521011.Mpal_2339; -.
DR   EnsemblBacteria; ACL17623; ACL17623; Mpal_2339.
DR   GeneID; 7272060; -.
DR   KEGG; mpl:Mpal_2339; -.
DR   eggNOG; arCOG01348; Archaea.
DR   HOGENOM; CLU_008831_0_2_2; -.
DR   OMA; VNLGHVG; -.
DR   OrthoDB; 104144at2157; -.
DR   Proteomes; UP000002457; 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: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..270
FT                   /note="NAD kinase"
FT                   /id="PRO_1000133576"
FT   ACT_SITE        63
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         63..64
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         131..132
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         142
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         172..177
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         230
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   270 AA;  29392 MW;  968C817E12C86B28 CRC64;
     MKLLLMSRID SEETLAYTRT LGIDLENVGF QIIYDTATAS ALEVNGVPLS SADPDAVVAI
     GGDGTILLCI QQMNIQRPII GINRGEVGFL ADLEPEEAFS FLKELKPGFP VERRMRIDLS
     VDGKPLGTAL NEAVIVTSRP AKMLRFSVLV DGVRAEQFRG DGLLISTPTG STAYAMSAGG
     PIIDPRIEGF LLVPLAPYML SSRPHLICAT RTLAVRLEAS KPAHLVLDGQ RTIDLGDQAT
     IEMTRSPEPA QFIDVNRNFF SKVEQKLRNL