YEGS_ALCBS
ID YEGS_ALCBS Reviewed; 300 AA.
AC Q0VSB2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable lipid kinase YegS-like {ECO:0000255|HAMAP-Rule:MF_01377};
DE EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_01377};
GN OrderedLocusNames=ABO_0488;
OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS SK2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=393595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX PubMed=16878126; DOI=10.1038/nbt1232;
RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA Weidner S., Kaiser O., Golyshin P.N.;
RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT Alcanivorax borkumensis.";
RL Nat. Biotechnol. 24:997-1004(2006).
CC -!- FUNCTION: Probably phosphorylates lipids; the in vivo substrate is
CC unknown. {ECO:0000255|HAMAP-Rule:MF_01377}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01377};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01377};
CC Note=Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute.
CC {ECO:0000255|HAMAP-Rule:MF_01377};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01377}.
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family. YegS
CC lipid kinase subfamily. {ECO:0000255|HAMAP-Rule:MF_01377}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAL15936.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM286690; CAL15936.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q0VSB2; -.
DR SMR; Q0VSB2; -.
DR STRING; 393595.ABO_0488; -.
DR EnsemblBacteria; CAL15936; CAL15936; ABO_0488.
DR KEGG; abo:ABO_0488; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_1_6; -.
DR OrthoDB; 869726at2; -.
DR Proteomes; UP000008871; 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:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10330; -; 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 Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR TIGRFAMs; TIGR03702; lip_kinase_YegS; 1.
DR TIGRFAMs; TIGR00147; TIGR00147; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..300
FT /note="Probable lipid kinase YegS-like"
FT /id="PRO_0000292139"
FT DOMAIN 1..129
FT /note="DAGKc"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT BINDING 64..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
SQ SEQUENCE 300 AA; 32576 MW; BC2A5CA96DFDD614 CRC64;
MSKKALLILH GKQADNQSVR NAVIDWRNQG HELAVRVTWE GGDAERYVRE ALDNGFKTII
AGGGDGSVRD ITQALMENGN SELELAIIPL GTANDFATAA EVSEEPADAL SLLNRPAQPC
DVIRVNNHYF LNMATGGFGT EVTTQTSEEL KKMLGGAAYL LTGLTRFSEI ESAKGHFKGE
DFEWEGDFLA LGLGNGRQAG GGQRLCPDAL VNDGLFDVAI LPADMDLLAG VKELFDSEAR
QDPDQEGLFV RTRLSEMKIE TPTPMNLNLD GEPIQNTTFQ IQAIRNALRL YLPEGCPLLG
