ID A8XZ66_CAEBR Unreviewed; 490 AA.
AC A8XZ66;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
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|WormBase:CBG21019a};
GN ORFNames=CBG21019 {ECO:0000313|EMBL:CAP37933.1,
GN ECO:0000313|WormBase:CBG21019a}, CBG_21019
GN {ECO:0000313|EMBL:CAP37933.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP37933.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP37933.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP37933.1,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE600928; CAP37933.1; -; Genomic_DNA.
DR RefSeq; XP_002631800.1; XM_002631754.1.
DR AlphaFoldDB; A8XZ66; -.
DR STRING; 6238.A8XZ66; -.
DR EnsemblMetazoa; CBG21019a.1; CBG21019a.1; WBGene00039904.
DR GeneID; 8573799; -.
DR KEGG; cbr:CBG_21019; -.
DR CTD; 8573799; -.
DR WormBase; CBG21019a; CBP11644; WBGene00039904; Cbr-nadk-2.
DR eggNOG; KOG4180; Eukaryota.
DR HOGENOM; CLU_039559_0_0_1; -.
DR InParanoid; A8XZ66; -.
DR OMA; LAGDFRW; -.
DR OrthoDB; 231143at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR017565}.
SQ SEQUENCE 490 AA; 55705 MW; 430C19B9C8F9B1B6 CRC64;
MRIRIRNIEQ VNQHLRNAYL CSTQPSVAPK VVVVPQSTIV DKGESSRYWV DPTNHMRLPR
SLAAALYQTQ NTQSKRSIGN MEKPSFQPKK VLILSKLTRY EFEKKVHKGC DDDQLASILK
KRGSDYQRLL SKHKIHHSYL NTLQKELENA GIESRLVRRF GYTQEAVDWA DAVFSAGGDG
TFLMASSKVR TKHKPVIGIN TDPQGSEGYM CLMRKLPEEN LSGALKKLFS GNFEWLYRQR
IRITVTGDDG ISDAIELHDQ QLNRDPATTR WTDNPRSPAR ENDVEECMSL SPPVKKRMIS
ESEDKAIVPI EKETVELPVL ALNEVFVGES LSSRVSYYEI GLNDEQMLKQ KSSGITICTG
TGSTSWHFNI NKLTEQCVQD LMKIVAQHCN LPQIPHENKN AVSEICTKFN QQLIFDPDRR
QLAFSVRDPI FNATFPPTDP RGFADKIRIK SRGYDAHLVI DGGISYRFND GSEAVMEVRD
EDTLRTVVFR
//
