ID A5P927_9SPHN Unreviewed; 226 AA.
AC A5P927;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:EDL49621.1};
GN ORFNames=ED21_18522 {ECO:0000313|EMBL:EDL49621.1};
OS Erythrobacter sp. SD-21.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL49621.1, ECO:0000313|Proteomes:UP000005498};
RN [1] {ECO:0000313|EMBL:EDL49621.1, ECO:0000313|Proteomes:UP000005498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD-21 {ECO:0000313|EMBL:EDL49621.1,
RC ECO:0000313|Proteomes:UP000005498};
RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:EDL49621.1}.
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DR EMBL; ABCG01000002; EDL49621.1; -; Genomic_DNA.
DR RefSeq; WP_006832654.1; NZ_ABCG01000002.1.
DR AlphaFoldDB; A5P927; -.
DR STRING; 161528.ED21_18522; -.
DR eggNOG; COG0204; Bacteria.
DR OrthoDB; 5290997at2; -.
DR Proteomes; UP000005498; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:EDL49621.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005498};
KW Transferase {ECO:0000313|EMBL:EDL49621.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..183
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 226 AA; 25207 MW; A888AD64CB443A26 CRC64;
MLLLRNLFFY PLFYLGSFLV TAASLASAPF SLAAFRRRVR NWGQWQRWCL KHIIGAEVVI
EGTPADKPVL YAIKHESFFE AIDAPNLLEC PSVFAKQELF AIPGWGRAAL AYGLIPVARD
KGAKMLMGMI RSAKKMVADG RPLVIFPEGT RIPHGERRQL QAGFAGLYKM LGLEVVPVAV
SSGEVYHRWL KKPGTITYRF GEPIPPGLPR EEIEARVLDA INALND
//
