ID G4F8X7_9GAMM Unreviewed; 221 AA.
AC G4F8X7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:EHA14879.1};
GN ORFNames=HAL1_14270 {ECO:0000313|EMBL:EHA14879.1};
OS Halomonas sp. HAL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA14879.1, ECO:0000313|Proteomes:UP000005692};
RN [1] {ECO:0000313|EMBL:EHA14879.1, ECO:0000313|Proteomes:UP000005692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX PubMed=22156396; DOI=10.1128/JB.06359-11;
RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA Wang G., Rensing C.;
RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL J. Bacteriol. 194:199-200(2012).
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:EHA14879.1}.
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DR EMBL; AGIB01000068; EHA14879.1; -; Genomic_DNA.
DR RefSeq; WP_008958732.1; NZ_CP130610.1.
DR AlphaFoldDB; G4F8X7; -.
DR PATRIC; fig|550984.5.peg.2750; -.
DR Proteomes; UP000005692; 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:SF15; PLSC DOMAIN-CONTAINING PROTEIN; 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:EHA14879.1};
KW Transferase {ECO:0000313|EMBL:EHA14879.1}.
FT DOMAIN 40..156
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 221 AA; 24937 MW; A590C824B4636552 CRC64;
MTGWVNVTRQ VLRWLIFISM RLCYRLQVHG RHHIPKHGAA LVVCNHVSFM DALVLGGASP
RPLRFVMDQP IFDSPWLKWW FQLVGAIPIE SERRSPGALR RALDDVSAAL RQGQVVMVFP
EGRLTPDGEI HAFRRGLETI LARDDVPVIP AGLAGLWGSW TSHHGGKALK KYPKRFRAPV
SLHFGPPLNR LDADDMALRR FLEARVRALK AAADQDLANR H
//
