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Database: UniProt
Entry: G3TLF4_LOXAF
LinkDB: G3TLF4_LOXAF
Original site: G3TLF4_LOXAF 
ID   G3TLF4_LOXAF            Unreviewed;       455 AA.
AC   G3TLF4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
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:ENSLAFP00000015718.3};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000015718.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000015718.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015718.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000015718.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015718.3};
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; XP_010586400.1; XM_010588098.1.
DR   AlphaFoldDB; G3TLF4; -.
DR   STRING; 9785.ENSLAFP00000015718; -.
DR   Ensembl; ENSLAFT00000020658.3; ENSLAFP00000015718.3; ENSLAFG00000005379.3.
DR   eggNOG; KOG4180; Eukaryota.
DR   GeneTree; ENSGT00390000006320; -.
DR   InParanoid; G3TLF4; -.
DR   OMA; LAGDFRW; -.
DR   TreeFam; TF314077; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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:UP000007646};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR017565}.
FT   REGION          23..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  51261 MW;  D23335A64225D718 CRC64;
     MTCYRGFLLG SCRRVAGGRA AALRGPGARG PAVRPRHLGQ GQPRELAGCG SRPDGGFRPS
     RVVVVAKTTR YEFEQQRYRY AELSEEDMKQ LLALKGSSYT GLLERHYIHT RNVEHIVDSL
     RNEGIEVRLV KRREYDEETV RWADAVIAAG GDGTMLLAAS KVLDRLKPVI GVNTDPERSE
     GHLCLPVRYT HAFPEALRKF YRGEFRWLWR QRIRLYLEGT GINPVPVDLH EQQLSLNQHS
     RAFNIERVHD EKSVASGPQL LPVRALNEVF IGESLSSRLS YSWAVAVDNL RRSIPTLKGL
     ASYYEISVDD GPWEKQKSSG LNLCTGTGSK AWSFNINRVA TQAVEDVLNI AKRQGSLSLP
     LNKELVEKVT NEYNESLLYS PEEPKILFSI REPIANRVFS SSRQRCFSSK VCVRSRCWDA
     CMVVDGGTSF EFNDGAIASM MINKEDELRT VLLEQ
//
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