ID A0A067R3G9_ZOONE Unreviewed; 364 AA. AC A0A067R3G9; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 22-FEB-2023, entry version 26. 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=ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N- CC hexanoylsphing-4-enine 1-phosphate; Xref=Rhea:RHEA:43312, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:63867, CC ChEBI:CHEBI:82959, ChEBI:CHEBI:456216; CC 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 monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3- CC phosphate; 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 = ADP + an N-acylsphing-4-enine CC 1-phosphate + 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: Membrane {ECO:0000256|ARBA:ARBA00004170}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}. CC Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}. CC -!- SIMILARITY: Belongs to the AGK family. {ECO:0000256|ARBA:ARBA00025749}. 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 EMBL; KK852936; KDR13605.1; -; Genomic_DNA. DR AlphaFoldDB; A0A067R3G9; -. DR STRING; 136037.KDR13605; -. DR EnsemblMetazoa; KDR13605; KDR13605; L798_12295. DR eggNOG; KOG4435; Eukaryota. DR OMA; YCEPILH; -. 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:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR InterPro; IPR045579; AGK_C. DR InterPro; IPR017438; ATP-NAD_kinase_N. DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom. DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf. DR PANTHER; PTHR12358:SF54; 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:0000313|EMBL:KDR13605.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Reference proteome {ECO:0000313|Proteomes:UP000027135}; KW Transferase {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 //