ID A0A074M7P1_ERYLO Unreviewed; 208 AA.
AC A0A074M7P1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:KEO88740.1};
GN ORFNames=EH31_14970 {ECO:0000313|EMBL:KEO88740.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO88740.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO88740.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO88740.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-2014) 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:KEO88740.1}.
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DR EMBL; JMIW01000007; KEO88740.1; -; Genomic_DNA.
DR RefSeq; WP_034961488.1; NZ_JMIW01000007.1.
DR AlphaFoldDB; A0A074M7P1; -.
DR STRING; 1044.EH31_14970; -.
DR eggNOG; COG0204; Bacteria.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000027647; Unassembled WGS sequence.
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:KEO88740.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027647};
KW Transferase {ECO:0000313|EMBL:KEO88740.1}.
FT DOMAIN 34..152
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 208 AA; 22177 MW; F7A22975D3393F20 CRC64;
MIAKLVGEAL FAAARFLVGG QARWRGCEPA TTQRIYFANH ASHMDTIIMC GALPGYLRTT
THPVAAADYW GSGPVQRFVA LKVLNAVLVE RGGAKDPLAP LREVLEQGES LIIFPEGTRR
AESLPGAFKA GLYHLAKDFP EAELVPVYLT NLARAYPKGA ILPAPISSAA HFGAPIQLED
SEDKAAFLAR AQASIIALSG EELPGENA
//
