ID E2C529_HARSA Unreviewed; 438 AA.
AC E2C529;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=EAI_12651 {ECO:0000313|EMBL:EFN76937.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN76937.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN76937.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 EMBL; GL452737; EFN76937.1; -; Genomic_DNA.
DR RefSeq; XP_011150869.1; XM_011152567.2.
DR AlphaFoldDB; E2C529; -.
DR STRING; 610380.E2C529; -.
DR EnsemblMetazoa; XM_011152567.3; XP_011150869.1; LOC105190072.
DR EnsemblMetazoa; XM_025307088.1; XP_025162873.1; LOC105190072.
DR GeneID; 105190072; -.
DR KEGG; hst:105190072; -.
DR InParanoid; E2C529; -.
DR OMA; DKYWYFG; -.
DR OrthoDB; 2907389at2759; -.
DR PhylomeDB; E2C529; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000008237; 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: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: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:0000313|EMBL:EFN76937.1};
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:UP000008237};
KW Transferase {ECO:0000313|EMBL:EFN76937.1}.
FT DOMAIN 61..209
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 438 AA; 49669 MW; 31E0825333040631 CRC64;
MAKALSLLKT IRNNWKKTLI GTAALSYGVS YGNQVYETGQ LMQQHCEEAA KYGDKPCPTN
VKPRHITVIL NPAAKKRKAK KLFEKYCVPL LHLAGIAVTI IDTQSGSHAR NAIINLETPT
DAIVVAGGDG TLSDVVTGLM RKYENNLQFV KQCPIGVLPL GNTNTIASKF FKNYTDLSDI
HHMIDATMAI VKNNFKLLDV LEIKVSEDNS DTSIKPVYAV GSIKWGAWSD IHGRIDKYWY
WGYLRKYAAY VFNGYKSDLN WKCNAVLKYT NPCKGCSHCY SKKISSDQTA NSNRRWWHAF
LPKTRTFIPD NHVDYSKVIN EDCGILHDLT VCTTEIHIKT ENANSKSASS IKVSIGPNDI
SYISFVEKGW DQERYDELDV VQPIVDAKYI ELYPEIKNEN QMFFIDHEEY ELKPIQIRLL
PKSITIFYPE SSKKTENV
//
