ID E8WMG1_GEOS8 Unreviewed; 217 AA.
AC E8WMG1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:ADW13771.1};
GN OrderedLocusNames=GM18_2312 {ECO:0000313|EMBL:ADW13771.1};
OS Geobacter sp. (strain M18).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW13771.1, ECO:0000313|Proteomes:UP000001442};
RN [1] {ECO:0000313|EMBL:ADW13771.1, ECO:0000313|Proteomes:UP000001442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M18 {ECO:0000313|EMBL:ADW13771.1,
RC ECO:0000313|Proteomes:UP000001442};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA Aklujkar M., Lovley D., Woyke T.;
RT "Complete sequence of Geobacter sp. M18.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141};
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DR EMBL; CP002479; ADW13771.1; -; Genomic_DNA.
DR AlphaFoldDB; E8WMG1; -.
DR STRING; 443143.GM18_2312; -.
DR KEGG; geb:GM18_2312; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_0_7; -.
DR OrthoDB; 9799237at2; -.
DR Proteomes; UP000001442; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:ADW13771.1};
KW Transferase {ECO:0000313|EMBL:ADW13771.1}.
FT DOMAIN 42..157
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 217 AA; 24296 MW; 0F055358A1E22B87 CRC64;
MKVSLLRCFW VTFSVWVIGC YASLLNRFRV EGAEVIPASG GVLIASNHIS AYDTIFLPWA
VIRSHPLQML WAPAKEELFQ NRVMGLVYRS WGAFPVRRGR DVRAGKHLNM LLADQKVMLF
PEGTRHKDGV LGKGNRGVGK IIYDTRPHVI PTALTGVNRW KFPGIGLKGG VTFGAPLDFS
DLYRLEDCKE THQMIVDRVM DAIALLLRQK EGDPHAG
//
