ID E7MLY8_9FIRM Unreviewed; 301 AA.
AC E7MLY8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Lipid kinase, YegS/Rv2252/BmrU family {ECO:0000313|EMBL:EFW24829.1};
DE EC=2.7.1.- {ECO:0000313|EMBL:EFW24829.1};
GN ORFNames=HMPREF9430_00551 {ECO:0000313|EMBL:EFW24829.1};
OS Solobacterium moorei F0204.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Solobacterium.
OX NCBI_TaxID=706433 {ECO:0000313|EMBL:EFW24829.1, ECO:0000313|Proteomes:UP000004097};
RN [1] {ECO:0000313|EMBL:EFW24829.1, ECO:0000313|Proteomes:UP000004097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0204 {ECO:0000313|EMBL:EFW24829.1,
RC ECO:0000313|Proteomes:UP000004097};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000256|ARBA:ARBA00005983}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFW24829.1}.
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DR EMBL; AECQ01000008; EFW24829.1; -; Genomic_DNA.
DR AlphaFoldDB; E7MLY8; -.
DR STRING; 706433.HMPREF9430_00551; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_0_9; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000004097; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
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 SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EFW24829.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004097};
KW Transferase {ECO:0000313|EMBL:EFW24829.1}.
FT DOMAIN 1..133
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 301 AA; 33050 MW; 478385F49927518B CRC64;
MKKKVMFLFN PEAGNNAIEK IVFDIIKNLT IFDCEVTVFP IMPDKGLGSE EILITHASEF
KTIVVYGGDG TLNRVVNIMM HQDIHLPIGY IPGGTTNDFS KAIDENGTIE SYCRTIAFGN
PFSYDVGCFN GTYFNYVAAF GAFTATSYET SRESKKILGY GAYVLNALGN LPASLSNHTK
MKFIHDGVEE EGTFVFGAIS NSPSVGGFKL PFYEDSTLDD GKFEVLLVAA LDNLEVLHNV
LSGVATGNIN PKYVHAFKTD KIEFICEEDT AWTLDGEDGG KHRLVTVEIH PKSMTIMTSK
S
//
