AGK_XENLA
ID AGK_XENLA Reviewed; 428 AA.
AC Q7ZYJ3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Acylglycerol kinase, mitochondrial {ECO:0000250|UniProtKB:Q53H12};
DE EC=2.7.1.107 {ECO:0000250|UniProtKB:Q53H12};
DE EC=2.7.1.138 {ECO:0000250|UniProtKB:Q9ESW4};
DE EC=2.7.1.94 {ECO:0000250|UniProtKB:Q53H12};
DE AltName: Full=Multiple substrate lipid kinase {ECO:0000250|UniProtKB:Q53H12};
DE Short=MuLK {ECO:0000250|UniProtKB:Q53H12};
DE Short=Multi-substrate lipid kinase {ECO:0000250|UniProtKB:Q53H12};
GN Name=agk {ECO:0000250|UniProtKB:Q53H12};
GN Synonyms=mulk {ECO:0000250|UniProtKB:Q53H12};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipid kinase that can phosphorylate both monoacylglycerol and
CC diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic
CC acid (PA), respectively (By similarity). Phosphorylates ceramide but
CC not sphingosine (By similarity). Phosphorylates 1,2-dioleoylglycerol
CC more rapidly than 2,3-dioleoylglycerol (By similarity). Independently
CC of its lipid kinase activity, acts as a component of the TIM22 complex
CC (By similarity). The TIM22 complex mediates the import and insertion of
CC multi-pass transmembrane proteins into the mitochondrial inner membrane
CC by forming a twin-pore translocase that uses the membrane potential as
CC the external driving force (By similarity).
CC {ECO:0000250|UniProtKB:Q53H12, ECO:0000250|UniProtKB:Q9ESW4}.
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19294;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q9ESW4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17930;
CC Evidence={ECO:0000250|UniProtKB:Q9ESW4};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41080;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33748;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43309;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43317;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q9ESW4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43329;
CC Evidence={ECO:0000250|UniProtKB:Q9ESW4};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43313;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000250|UniProtKB:Q53H12}.
CC -!- SUBUNIT: Component of the TIM22 complex.
CC {ECO:0000250|UniProtKB:Q53H12}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q53H12}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q53H12}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q53H12}. Note=Localizes in the mitochondrion
CC intermembrane space, where it associates with the inner membrane. It is
CC unclear whether the N-terminal hydrophobic region forms a transmembrane
CC region or associates with the membrane without crossing it.
CC {ECO:0000250|UniProtKB:Q53H12}.
CC -!- SIMILARITY: Belongs to the AGK family. {ECO:0000305}.
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; BC043761; AAH43761.1; -; mRNA.
DR RefSeq; NP_001079476.1; NM_001086007.1.
DR AlphaFoldDB; Q7ZYJ3; -.
DR SMR; Q7ZYJ3; -.
DR DNASU; 379163; -.
DR GeneID; 379163; -.
DR KEGG; xla:379163; -.
DR CTD; 379163; -.
DR Xenbase; XB-GENE-979728; agk.S.
DR OrthoDB; 1312024at2759; -.
DR BRENDA; 2.7.1.107; 6725.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 379163; Expressed in blastula and 19 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; ISS:UniProtKB.
DR GO; GO:0047620; F:acylglycerol kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001729; F:ceramide kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004143; F:diacylglycerol kinase activity; ISS:UniProtKB.
DR GO; GO:0102773; F:dihydroceramide kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:UniProtKB.
DR Gene3D; 3.40.50.10330; -; 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 Pfam; PF19712; AGK_C; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..428
FT /note="Acylglycerol kinase, mitochondrial"
FT /id="PRO_0000252384"
FT DOMAIN 61..202
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REGION 18..34
FT /note="Hydrophobic"
FT /evidence="ECO:0000250|UniProtKB:Q53H12"
SQ SEQUENCE 428 AA; 47962 MW; 5B883EF39E042922 CRC64;
MARVVRIFKT LRNHWKKSTV GFCLLAYGSH WLYGKHCDNL LRRAACEEAQ VFGNHQILPH
SAIKKATVFL NPAACKGKAR TLFEKNAAPV LHLAGIDITV VKTDYEGQAK KLLELMEKTD
LIIVAGGDGT VQEVITGLLR RDDEASFSKI PIGFIPLGGT NTLSHTLYPE RENKVEQITE
ATLSILKGET VPLDVLQIKG EQDQPVFAVQ GIRWGSYRDA SVKVSKYWYL GPLKARAAHL
FSALKEWPQQ HQASISYLGP AERPPEEPEQ KPSRPPLYVR IYRRLALYWS PPKVEVPVEP
TPEPWEEAQL SAVELSITTQ NHQPDLLRTL DSMSIHIEPD TISKGKFIQL GAQKMTDPLL
HPEDSQVLLA SRCSLHLPQG TEGHFSIDSE EYEAMSVDVT LLPRKLHFLC HPTRKQELLQ
SPTATAQS
