ID A0A0A2W1R8_BEABA Unreviewed; 302 AA.
AC A0A0A2W1R8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN ORFNames=BBAD15_g1883 {ECO:0000313|EMBL:KGQ12380.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ12380.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ12380.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ12380.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361267};
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC ECO:0000256|RuleBase:RU361267}.
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:KGQ12380.1}.
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DR EMBL; ANFO01000123; KGQ12380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2W1R8; -.
DR STRING; 1245745.A0A0A2W1R8; -.
DR eggNOG; KOG2848; Eukaryota.
DR HOGENOM; CLU_027938_10_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:EnsemblFungi.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF11; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE ALPHA; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW ECO:0000313|EMBL:KGQ12380.1};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:KGQ12380.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 103..220
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 280..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 33141 MW; D63C5C3725CB340D CRC64;
MNAFLYYTVA AFVAYCALTS ALFMLSFIVP RAGFFARCLA MYMTFFGAAV FGVVSSIILT
LLGQQNIAQW ATARAFLYAA RLTTGTSFEV DDPTNILGTT RPAVFIGNHQ TELDVLMLGA
VFPKYCSVTG KRSLKHIPFL GWFMTLSGSI FIDRANSKDA RQAMQGAADE IKARKQSVYM
FPEGTRSYSK EPTLLPFKKG AFHLAVQAGV PIVPCVVANY SHLLYPKEYR FNAGTFTNMP
CQVLDPIPTK NLTSADVDEL TRTTRELMLK ELMTLTAKAR GQPMAVPANP TSAKSSGVDL
KN
//