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Database: UniProt
Entry: Q16Y30_AEDAE
LinkDB: Q16Y30_AEDAE
Original site: Q16Y30_AEDAE 
ID   Q16Y30_AEDAE            Unreviewed;       436 AA.
AC   Q16Y30;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   24-JAN-2024, entry version 105.
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=AAEL008676 {ECO:0000313|EMBL:EAT39530.1};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT39530.1, ECO:0000313|Proteomes:UP000682892};
RN   [1] {ECO:0000313|EMBL:EAT39530.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT39530.1};
RA   Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA   Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA   Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA   Rogers Y.-H., Kravitz S., Fraser C.M.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAT39530.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT39530.1};
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
RN   [3] {ECO:0000313|EMBL:EAT39530.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT39530.1};
RG   VectorBase;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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; CH477526; EAT39530.1; -; Genomic_DNA.
DR   RefSeq; XP_001653417.1; XM_001653367.1.
DR   AlphaFoldDB; Q16Y30; -.
DR   STRING; 7159.Q16Y30; -.
DR   PaxDb; 7159-AAEL008676-PA; -.
DR   GeneID; 5570950; -.
DR   KEGG; aag:5570950; -.
DR   VEuPathDB; VectorBase:AAEL008676; -.
DR   eggNOG; KOG4435; Eukaryota.
DR   HOGENOM; CLU_042458_2_0_1; -.
DR   OMA; DKYWYFG; -.
DR   OrthoDB; 2907389at2759; -.
DR   PhylomeDB; Q16Y30; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000682892; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}.
FT   DOMAIN          61..205
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   436 AA;  49059 MW;  07FECD2EB83DD019 CRC64;
     MAFVIRFAKG VRNHWKKSTF LASAVAYGVS YSHEKYEIKQ LMRHYCTEAS KYGDIVVGKT
     QRLQKVLVLL NPAANRKSCE EDFHDYCEPI LHLAGFEVDI VKTDSEGHAR RYLEELATLP
     DAIVVAGGDG TVSEVVSGLK RRGDGAECPI GVLPVGRTNG LAMALFRSSE DTSKLEDVRA
     MANAAYAVVA GKKEKMDLMK IEVLPNEIDE KVPEKPVYAV GSVHWGAFRD ILALRDKYWY
     TGSLRDYTAF LFNLFDGKHT WNCKAKVTYT EPCQGCSKCY QEHQQQPKQE PTRRWWSVFI
     PKAKTAQGVD YSKVVNAKCS VPFELEVDAA ELVLQTTNAD LSGSKESDSK LCVKIGTPVD
     SVFSFLSDSW SRIWNRKFVH CPTEKTVEAR TVYLIPEKLK PDEGDSEAYY SIDNEAYEVR
     PVRVTLVPRA VEVFTF
//
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