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Database: UniProt
Entry: A0A2K5HG71_COLAP
LinkDB: A0A2K5HG71_COLAP
Original site: A0A2K5HG71_COLAP 
ID   A0A2K5HG71_COLAP        Unreviewed;       244 AA.
AC   A0A2K5HG71;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000003349.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000003349.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A2K5HG71; -.
DR   SMR; A0A2K5HG71; -.
DR   Ensembl; ENSCANT00000013407.1; ENSCANP00000003349.1; ENSCANG00000011634.1.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000233080; Unplaced.
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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT   DOMAIN          58..196
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   244 AA;  26925 MW;  4BB4065BE132335E CRC64;
     MTVFFKTLRN HWKKTTAGLC LLTWGGHWLY GKHCDNLLRR AACQEAQVFG NQLIPPNAQV
     KKATVFLNPA ACKGTLFEKN AAPILHLSGM DVTIVKTDYE GQAKKLLELM ENTDVIIVAG
     GDGTLQEVVT GVLRRTDEAT FSKIPIGFIP LGETSSLSHT LFAESGNKVQ HITDATLAIV
     KGETVPLDVL QIKGEKEQPV FAMTGLRWGS FRDAGVKVSK YWYLGPLKIK AAHFFSTLKP
     FPKR
//
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