ID K0CK59_ALCDB Unreviewed; 305 AA.
AC K0CK59;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Probable lipid kinase YegS-like {ECO:0000256|HAMAP-Rule:MF_01377};
DE EC=2.7.1.- {ECO:0000256|HAMAP-Rule:MF_01377};
GN OrderedLocusNames=B5T_03688 {ECO:0000313|EMBL:AFT71951.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT71951.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT71951.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(2012).
CC -!- FUNCTION: Probably phosphorylates lipids; the in vivo substrate is
CC unknown. {ECO:0000256|HAMAP-Rule:MF_01377}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01377};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01377};
CC Note=Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute.
CC {ECO:0000256|HAMAP-Rule:MF_01377};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01377}.
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family. YegS
CC lipid kinase subfamily. {ECO:0000256|HAMAP-Rule:MF_01377}.
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DR EMBL; CP003466; AFT71951.1; -; Genomic_DNA.
DR RefSeq; WP_014996010.1; NC_018691.1.
DR AlphaFoldDB; K0CK59; -.
DR STRING; 930169.B5T_03688; -.
DR KEGG; adi:B5T_03688; -.
DR PATRIC; fig|930169.3.peg.3639; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_1_6; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000006286; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001727; F:lipid kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR HAMAP; MF_01377; YegS; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR022433; Lip_kinase_YegS.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR NCBIfam; TIGR03702; lip_kinase_YegS; 1.
DR NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
DR PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01377}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01377};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01377};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01377};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01377};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01377};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01377};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01377};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01377};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01377};
KW Reference proteome {ECO:0000313|Proteomes:UP000006286};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01377}.
FT DOMAIN 1..129
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 65..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
SQ SEQUENCE 305 AA; 32375 MW; 34289F7E1AA143C5 CRC64;
MVSAKALLIL HGKQATNDEV RQAVMARREQ GHQLDVRVTW EGGDAERYVE EALNAGYDTV
IAGGGDGSVR DITDTLMKNG GGANLGILPL GTANDFATAA NIPVPPKDAL ALLDQPATAI
DVLEVNGHYF LNMATGGFGT EVTTETSEEL KSMLGGAAYL LTGLTRFTEI RSAQGHFRGQ
DFEWEGEFMA LGVGNGRQAG GGQKLCPDAV INDGLMDVAI LPAQMDLMSG LRGLFSSDDG
ANGNNGNGEQ EGLFVRARLA SMEIRTPEAM YLNLDGEPLE DTHFHIKVHA GALRVHLSPD
TPLLS
//
