ID I3JVU4_ORENI Unreviewed; 365 AA.
AC I3JVU4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 56.
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 Name=agk {ECO:0000313|Ensembl:ENSONIP00000012989.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000012989.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000012989.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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-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}.
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DR AlphaFoldDB; I3JVU4; -.
DR STRING; 8128.ENSONIP00000050613; -.
DR Ensembl; ENSONIT00000012999.2; ENSONIP00000012989.2; ENSONIG00000010333.2.
DR eggNOG; KOG4435; Eukaryota.
DR GeneTree; ENSGT00940000154961; -.
DR HOGENOM; CLU_042458_0_0_1; -.
DR TreeFam; TF320485; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000005207; Linkage group LG7.
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:InterPro.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
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:SF116; ACYLGLYCEROL KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF19712; AGK_C; 2.
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 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:UP000005207}.
FT DOMAIN 55..196
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 365 AA; 41693 MW; 094617C51C5F53E9 CRC64;
MARVVKVFRT LRNHWKKSTF AVCVLSYGGY WLYGKHWWVF HAMNETECTN SPPQERIRKA
TVILNPAACN GKANNLFEKN AAPILHLAGV QITVVKTDYE GQAKKLIELM EETDMLIVAG
GDGTLQEVIT GLLRRPDQDV FSKTPIGFIP LGSHNSLSPS LHLLSDNKVK DITSATLSIL
KGETVPLDVL QIKGEKEQPV FALMGLRWGA FRDVASKISK YWYLGPLKTN AAHWFSTLRE
WPLVRDVSVS YLAPTLRPPD LPPVKAPRPN LIYRIIRRLK NYWNPPAEEP PKVEEPEKWE
EQQLSTLELF IQTHNKNPVE RGASGFYNID NEEYEAMPVE VRLLPRKLRF FISAERREQL
LSQIQ
//
