ID A0A182XMF6_ANOQN Unreviewed; 446 AA.
AC A0A182XMF6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA011052-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA011052-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA011052-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; A0A182XMF6; -.
DR STRING; 34691.A0A182XMF6; -.
DR EnsemblMetazoa; AQUA011052-RA; AQUA011052-PA; AQUA011052.
DR VEuPathDB; VectorBase:AQUA011052; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000076407; 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:InterPro.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01653; GATase1; 1.
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; 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 Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}.
FT DOMAIN 61..206
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 446 AA; 49952 MW; B6BB8F2EFC4A3408 CRC64;
MAFVIRFAKA VRNNWKKSTV FGSALAYGVS YSNEKYEIKQ LMRYYCTEAS RYGDVKINLN
QRPPKVLVLL NPAANRKSSE EDFHDYCEPI LHLAGFEVDL VKTDSEGHAR RYVEELATLP
DALIVGGGDG TLSEAVSGMK RRQDGAQCPI GVLPLGRTNT LAMKLFSAEG SSNSDLEHVR
TMANAAYAVI AGKKEKTDIM RIEVLPSAAD ETPPEKPVYA VGALQWGAFR DILALRDKYW
YTASLRDYTA FLFNAFDGKH TWSCKAKIAY TEPCSGCSNC YKDMDDQWTA AKKAEQQPRR
WWSVFVPRAK TAAKTDYSKI INEKCSVRHE IEVEPSELVI KTGNVAADEQ EGEKGTDSTK
LDVVVGEQVD SSFGFIGGSW GRVRGRKYFD CPAKDSISVR TVELLPERLK VEETDPELYY
SIDNEAYEVR PVRITVVPKA VEIFTF
//
