ID A0A2G5V6H0_9PELO Unreviewed; 490 AA.
AC A0A2G5V6H0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 15.
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=Cni-Y17G7B.10 {ECO:0000313|EMBL:PIC47404.1};
GN Synonyms=Cnig_chr_II.g6777 {ECO:0000313|EMBL:PIC47404.1};
GN ORFNames=B9Z55_006777 {ECO:0000313|EMBL:PIC47404.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC47404.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC47404.1}.
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DR EMBL; PDUG01000002; PIC47404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5V6H0; -.
DR STRING; 1611254.A0A2G5V6H0; -.
DR Proteomes; UP000230233; Chromosome ii.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019674; P:NAD metabolic process; IEA:UniProtKB-UniRule.
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:UP000230233};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR017565}.
SQ SEQUENCE 490 AA; 55691 MW; CA989ECB1970BB2F CRC64;
MRIRIRNIEQ VNQHLRNAYL CSTQPSVAPK AVVVPQSTIV DKGESSRYWV DPTNHMRLPR
SLAAALYQTQ NTQSKRSIGN MEKPSFQPKK VLILSKLTRY EFEKKVHKGC DDDQLASILK
KRGSDYQRLL SKHKIHHSYL NTLQKELENA GIESRLVRRF GYTQEAVDWA DAVFSAGGDG
TFLMASSRVR TKHKPVIGIN TDPQGSEGYM CLMRKLPEEN LSGALKKLFS GNFEWLYRQR
IRITVTGDDG ISDAIELHDQ QLNRDPATTR WTDNPRSPAR ENDVEECMSL SPPVKKRMIS
ESEDKAIVPI EKETVELPVL ALNEVFVGES LSSRVSYYEI GLNDEQMLKQ KSSGITICTG
TGSTSWHFNI NKLTEQCVQD LMKIVAQHCN LPQIPHDNKN AVSEICTKFN QQLIFDPDRR
QLAFSVRDPI FNATFPPTDP RGFADKIRIK SRGYDAHLVI DGGISYRFND GSEAVMEVRD
EDTLRTVVFR
//
