ID   A0A1I7YID4_9BILA        Unreviewed;       449 AA.
AC   A0A1I7YID4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 21.
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};
OS   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g16684.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g16684.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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|PIRNR:PIRNR017565}.
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   AlphaFoldDB; A0A1I7YID4; -.
DR   WBParaSite; L893_g16684.t1; L893_g16684.t1; L893_g16684.
DR   Proteomes; UP000095287; Unplaced.
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; IPR012355; NADK2_mit.
DR   PANTHER; PTHR13158; -; 1.
DR   PANTHER; PTHR13158:SF5; NAD KINASE 2, MITOCHONDRIAL; 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|PIRNR:PIRNR017565};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR017565};
KW   NAD {ECO:0000256|PIRNR:PIRNR017565}; NADP {ECO:0000256|PIRNR:PIRNR017565};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017565};
KW   Transferase {ECO:0000256|PIRNR:PIRNR017565}.
SQ   SEQUENCE   449 AA;  50525 MW;  AD4B4827C36AC342 CRC64;
     MHSLSVCAVK CVSAYASAVL KNGFPAACRR QLTTNSRQFV GHLNDDIALG SAMPNSTHDG
     CCESGTAVAN GSDTDTQKME FNPKRVLLLS KITRLEFERR RHPNLNESEL ELLLKTRGSD
     YERLLNKHNH HLSYLNLINS ELNRAGIETR IVKRFNYTDD VIDWADAIFS AGGDGTFLLA
     ASKIKTRDKA VIGINTDPTG SEGYMCLMRK KPADAFPEAL QRLLSGDFRW LWRQRIRISL
     VNGRLDDPVE LHDQELHVDI DEVRARQSST TLSSEHRYPL LSLNEVYIGE SQSSRVSYYE
     LQLDSQPMVK QKSSGITICT GTGSTSWHFN INKLTNECVS ELLNILNGTF NTAVEPTKDN
     VQKIVDQFNS RLVYEPDCKK MAYSVRDAIW NATFPRLPPR GFAERIRVKS RCFDANLVID
     GGISYKFNDG MEAVLEMHPE DALRTVILG
//