ID D7NC29_9BACT Unreviewed; 252 AA.
AC D7NC29;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acetyltransferase {ECO:0000313|EMBL:EFI48717.1};
GN ORFNames=HMPREF0665_01092 {ECO:0000313|EMBL:EFI48717.1};
OS Segatella oris C735.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=563008 {ECO:0000313|EMBL:EFI48717.1, ECO:0000313|Proteomes:UP000003805};
RN [1] {ECO:0000313|EMBL:EFI48717.1, ECO:0000313|Proteomes:UP000003805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 {ECO:0000313|EMBL:EFI48717.1,
RC ECO:0000313|Proteomes:UP000003805};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella oris strain C735.";
RL Submitted (FEB-2010) 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; GL349566; EFI48717.1; -; Genomic_DNA.
DR RefSeq; WP_004377374.1; NZ_GL349566.1.
DR AlphaFoldDB; D7NC29; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_6_3_10; -.
DR Proteomes; UP000003805; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003805};
KW Transferase {ECO:0000313|EMBL:EFI48717.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..188
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 252 AA; 29040 MW; A86904AB46D4D6C6 CRC64;
MKYLYRLYQL FICLPILLLA SIITSLVTVI GCLVGNGHFW GYYPGKCWAW LWIRLLLLPV
KVEGREHLAP RQSYVFVANH QGAFDIFLIY GFLGRNFKWM MKKGLRKIPL VGIACQYAHH
IFVDKSGPSK IRATYDEARH ILQEGMSLVV FPEGARTFTG HMGVFRRGAF MLADDLQLPV
VPLTINGSFD VKPRTKDFYW AFWHPLKLTI HEPIMPIGRG PENIKNQMEQ SYEAVMNGLD
KEYQGFVENP DQ
//
