ID   A0A067R3G9_ZOONE        Unreviewed;       364 AA.
AC   A0A067R3G9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-NOV-2024, entry version 33.
DE   RecName: Full=Acylglycerol kinase, mitochondrial {ECO:0000256|ARBA:ARBA00026142};
DE            EC=2.7.1.107 {ECO:0000256|ARBA:ARBA00012133};
DE            EC=2.7.1.138 {ECO:0000256|ARBA:ARBA00026096};
DE            EC=2.7.1.94 {ECO:0000256|ARBA:ARBA00026098};
DE   AltName: Full=Multiple substrate lipid kinase {ECO:0000256|ARBA:ARBA00030553};
GN   ORFNames=L798_12295 {ECO:0000313|EMBL:KDR13605.1};
OS   Zootermopsis nevadensis (Dampwood termite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Termopsidae; Zootermopsis.
OX   NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR13605.1, ECO:0000313|Proteomes:UP000027135};
RN   [1] {ECO:0000313|EMBL:KDR13605.1, ECO:0000313|Proteomes:UP000027135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KDR13605.1};
RX   PubMed=24845553; DOI=10.1038/ncomms4636;
RA   Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA   Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA   Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA   Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA   Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA   Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA   Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA   Liebig J.;
RT   "Molecular traces of alternative social organization in a termite genome.";
RL   Nat. Commun. 5:3636-3636(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00023371};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC         Evidence={ECO:0000256|ARBA:ARBA00023371};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-
CC         (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:43328, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:34071, ChEBI:CHEBI:74938, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00024483};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43329;
CC         Evidence={ECO:0000256|ARBA:ARBA00024483};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-
CC         sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41079,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:74544,
CC         ChEBI:CHEBI:75757, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00024505};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41080;
CC         Evidence={ECO:0000256|ARBA:ARBA00024505};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-
CC         3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43308, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57518, ChEBI:CHEBI:75542,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024636};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43309;
CC         Evidence={ECO:0000256|ARBA:ARBA00024636};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-
CC         (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:43316, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:52392, ChEBI:CHEBI:78209, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00024556};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43317;
CC         Evidence={ECO:0000256|ARBA:ARBA00024556};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(hexanoyl)sphing-4-enine + ATP = N-hexanoylsphing-4-enine 1-
CC         phosphate + ADP + H(+); Xref=Rhea:RHEA:43312, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63867, ChEBI:CHEBI:82959,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024616};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43313;
CC         Evidence={ECO:0000256|ARBA:ARBA00024616};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC         phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC         ChEBI:CHEBI:456216; EC=2.7.1.107;
CC         Evidence={ECO:0000256|ARBA:ARBA00023411};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC         Evidence={ECO:0000256|ARBA:ARBA00023411};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate +
CC         ADP + H(+); Xref=Rhea:RHEA:33747, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024512};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33748;
CC         Evidence={ECO:0000256|ARBA:ARBA00024512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-acylglycerol + ATP = a 2-acyl-sn-glycerol 3-phosphate +
CC         ADP + H(+); Xref=Rhea:RHEA:39847, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17389, ChEBI:CHEBI:30616, ChEBI:CHEBI:64982,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00044480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39848;
CC         Evidence={ECO:0000256|ARBA:ARBA00044480};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monoacylglycerol + ATP = a monoacyl-sn-glycero-3-phosphate +
CC         ADP + H(+); Xref=Rhea:RHEA:19293, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:30616, ChEBI:CHEBI:77589,
CC         ChEBI:CHEBI:456216; EC=2.7.1.94;
CC         Evidence={ECO:0000256|ARBA:ARBA00024567};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19294;
CC         Evidence={ECO:0000256|ARBA:ARBA00024567};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + ATP = an N-acylsphing-4-enine 1-
CC         phosphate + ADP + H(+); Xref=Rhea:RHEA:17929, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674,
CC         ChEBI:CHEBI:456216; EC=2.7.1.138;
CC         Evidence={ECO:0000256|ARBA:ARBA00024607};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17930;
CC         Evidence={ECO:0000256|ARBA:ARBA00024607};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00005175}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004637}. Mitochondrion intermembrane space
CC       {ECO:0000256|ARBA:ARBA00004569}.
CC   -!- SIMILARITY: Belongs to the AGK family. {ECO:0000256|ARBA:ARBA00025749}.
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DR   EMBL; KK852936; KDR13605.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067R3G9; -.
DR   STRING; 136037.A0A067R3G9; -.
DR   EnsemblMetazoa; KDR13605; KDR13605; L798_12295.
DR   eggNOG; KOG4435; Eukaryota.
DR   InParanoid; A0A067R3G9; -.
DR   OMA; DKYWYFG; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000027135; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0047620; F:acylglycerol kinase activity; IEA:TreeGrafter.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:TreeGrafter.
DR   GO; GO:0001729; F:ceramide kinase activity; IEA:TreeGrafter.
DR   GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IEA:TreeGrafter.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IEA:TreeGrafter.
DR   InterPro; IPR045579; AGK_C.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR050187; Lipid_Phosphate_FormReg.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   PANTHER; PTHR12358:SF116; ACYLGLYCEROL KINASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF19712; AGK_C; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KDR13605.1};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KDR13605.1}.
FT   DOMAIN          61..205
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   364 AA;  40650 MW;  0D8F8AD19B72651E CRC64;
     MARIVKALTA VRNNWKKSVF ICAAASYGLQ YAVDKYNSFQ LMRGYCEEAL QYGEIPVLNG
     SRPRHITIIL NPVANKRKSK KNFDKYCAPL LHLAGISVNI IQTESEGQAR GLVESLDEVV
     DAIVIAGGDG TVSEAVTGLL RRADGDLAVQ RKFPIGILPL GRTNTVGTSL FFDSDKVKMM
     AEATMAVVKE ITKPVDVIKI EVLETEQELP GKAVYCLGGI QWGAYRDAHA KRDKYWYWGA
     LRSYVTYVFT GLKSDESDVS WQCKGVLSYI LPCSGCSRCI QPVETDTSTR RWWHVFVSRQ
     IVEPVSKDYS KVINEHCGTK LQKEISAVDL SLTTANVSPN CFRDGDPHIK VELGKDFMYK
     FHPY
//