ID Q9XXI5_CAEEL Unreviewed; 492 AA.
AC Q9XXI5;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=NAD kinase 2, mitochondrial {ECO:0000256|PIRNR:PIRNR017565};
DE EC=2.7.1.23 {ECO:0000256|PIRNR:PIRNR017565};
DE AltName: Full=NAD kinase domain-containing protein 1, mitochondrial {ECO:0000256|PIRNR:PIRNR017565};
GN Name=nadk-2 {ECO:0000313|EMBL:CAA19456.1,
GN ECO:0000313|WormBase:Y17G7B.10b};
GN ORFNames=CELE_Y17G7B.10 {ECO:0000313|EMBL:CAA19456.1}, Y17G7B.10
GN {ECO:0000313|WormBase:Y17G7B.10b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA19456.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA19456.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA19456.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to
CC yield NADP(+). Can use both ATP or inorganic polyphosphate as the
CC phosphoryl donor. {ECO:0000256|PIRNR:PIRNR017565}.
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|PIRNR:PIRNR017565};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR017565}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR017565}.
CC -!- SIMILARITY: Belongs to the NAD kinase family.
CC {ECO:0000256|ARBA:ARBA00010995, ECO:0000256|PIRNR:PIRNR017565}.
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DR EMBL; BX284602; CAA19456.1; -; Genomic_DNA.
DR PIR; T26502; T26502.
DR RefSeq; NP_496566.1; NM_064165.5.
DR AlphaFoldDB; Q9XXI5; -.
DR SMR; Q9XXI5; -.
DR STRING; 6239.Y17G7B.10b.3; -.
DR EPD; Q9XXI5; -.
DR PaxDb; 6239-Y17G7B-10b-1; -.
DR PeptideAtlas; Q9XXI5; -.
DR EnsemblMetazoa; Y17G7B.10b.1; Y17G7B.10b.1; WBGene00012463.
DR GeneID; 174846; -.
DR KEGG; cel:CELE_Y17G7B.10; -.
DR UCSC; Y17G7B.10a.2; c. elegans.
DR AGR; WB:WBGene00012463; -.
DR WormBase; Y17G7B.10b; CE19044; WBGene00012463; nadk-2.
DR eggNOG; KOG4180; Eukaryota.
DR InParanoid; Q9XXI5; -.
DR OMA; LAGDFRW; -.
DR OrthoDB; 231143at2759; -.
DR PhylomeDB; Q9XXI5; -.
DR Reactome; R-CEL-196807; Nicotinate metabolism.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00012463; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; Q9XXI5; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003951; F:NAD+ kinase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019674; P:NAD metabolic process; IBA:GO_Central.
DR GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR012355; NADK2_mit.
DR PANTHER; PTHR13158; -; 1.
DR PANTHER; PTHR13158:SF5; NAD KINASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF01513; NAD_kinase; 1.
DR PIRSF; PIRSF017565; Kin_ATP-NAD_euk; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR017565};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR017565};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR017565};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR017565};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR017565};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017565};
KW Proteomics identification {ECO:0007829|EPD:Q9XXI5,
KW ECO:0007829|PeptideAtlas:Q9XXI5};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR017565}.
SQ SEQUENCE 492 AA; 55416 MW; B3EB4F15721738AF CRC64;
MRIRIRSQHV EQLNQHVRNA YLCSSQPSVA PRIATAAAGA VVAPLPVKDE SSRYWVDPTN
HMRLPRSLAA ALYQTQNTQS KRSIGNMEKP SFTPKKVLIL SKLTRYEFEK RVNKGCSDEQ
LATLLKKRGS DYGRLLSKHK IHHSYLNTLQ RELENAGIES RLVRRFGYTQ EAVDWADAVF
SAGGDGTFLM ASSRVRTKHK PVIGINTDPQ GSEGYMCLMR KLPEENLAGA LKKLFSGNFE
WLNRQRIRIT VTGDDGISDA IELHDQQLNR DPATTRWTDN PRSPAREIEE CMSLSPPVKK
RMISEAVEIP EVEKETVELP VLALNEVFIG ESLSSRVSYY EIGINDAQML KQKSSGITIC
TGTGSTSWNF NINKLTEQCV QDLMKIVAEH CNLPQIPHGD KNAVSEICTK FNQQLIFDPD
RKQLAFSVRD PIFNATFPPT DPRGFADKIC IKSRGYDAHL VIDGGISYRF NDGSEAVMEV
RDEDTLRTVV FR
//
