ID A0A3Q1MUI7_BOVIN Unreviewed; 442 AA.
AC A0A3Q1MUI7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=NADK2 {ECO:0000313|Ensembl:ENSBTAP00000074248.1,
GN ECO:0000313|VGNC:VGNC:31864};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000074248.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000074248.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000074248.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000074248.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000074248.1};
RG Ensembl;
RL Submitted (NOV-2023) 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|ARBA:ARBA00010995, ECO:0000256|PIRNR:PIRNR017565}.
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DR RefSeq; NP_001243482.1; NM_001256553.2.
DR AlphaFoldDB; A0A3Q1MUI7; -.
DR Ensembl; ENSBTAT00000072737.1; ENSBTAP00000074248.1; ENSBTAG00000011334.6.
DR GeneID; 506968; -.
DR KEGG; bta:506968; -.
DR CTD; 133686; -.
DR VEuPathDB; HostDB:ENSBTAG00000011334; -.
DR VGNC; VGNC:31864; NADK2.
DR GeneTree; ENSGT00390000006320; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000011334; Expressed in oocyte and 109 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1MUI7; baseline and differential.
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 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|PeptideAtlas:A0A3Q1MUI7};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR017565}.
FT REGION 26..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 49760 MW; F051982899B9E53D CRC64;
MTCYRGFLLG SCRRVAGGRA AVLRGPGAGG PTARPWLGGE GGSRRHLGQG QPRELAGCGS
RPDGGFRPSR VVVVAKTTRY EFEQQRYRYA ELSEEDLKQL LALKGSSYSG LLERHHIHTK
NVEHILDSLR NEGIEVRLVK RREYDEETVR WADAVIAAGG DGTMLLAASK VLDRLKPVIG
VNTDPERSEG HLCLPVRYTH SFPEALQKFY RGEFRWLWRQ RIRLYLEGTG INPIPVDLHE
QQLSLNQHSR AFNIERVHDE RFEASGPQLL PVRALNEVFI GESLSSRASY YEISVDDGPW
EKQKSSGLNL CTGTGSKAWS FNINRVAPQA VEDVLNIANR QGNLSLPLNR ELVEKVTNEY
NESLLYSPEE PKILFSIREP IANRIFSSSR QRCFTSKVCV RSRCWDACMV VDGGTSFEFN
DGAIASMLIE KEDELRTVLL EQ
//
