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Database: UniProt
Entry: A0A0D2FXY2_9EURO
LinkDB: A0A0D2FXY2_9EURO
Original site: A0A0D2FXY2_9EURO 
ID   A0A0D2FXY2_9EURO        Unreviewed;       294 AA.
AC   A0A0D2FXY2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=PV04_01491 {ECO:0000313|EMBL:KIW73363.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW73363.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW73363.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW73363.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; KN846956; KIW73363.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2FXY2; -.
DR   STRING; 5601.A0A0D2FXY2; -.
DR   HOGENOM; CLU_027938_10_0_1; -.
DR   OrthoDB; 209232at2759; -.
DR   Proteomes; UP000054266; Unassembled WGS sequence.
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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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   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:UP000054266};
KW   Transferase {ECO:0000256|RuleBase:RU361267};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..226
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   294 AA;  32963 MW;  B679039BB1665D34 CRC64;
     MFFLLRWTLY FLSFYLFTML SFFALHTYLP GPPQILGFIA RTMAAYLSLI ACAAYGTIAS
     AILRPFGLHF AYGQWTTAKA FKNLCIYTLG VKFEILDNGE QILNNTRPAV FIVNHQTELD
     VLLLGWIWPK NCSVTAKKSL RSIPFLGWFM TLSGTIFIDR VDRSAAMKAF EGAAKAMKEK
     RQSVVIFPEG TRSYSLEPML LPFKKGAFHL AVQGGVDIVP VVAENYSAVL SPKLKRFNAG
     TIRVKVLDPI PTKGLTAADV DQLTRDTREK MLKVITAMGQ DPESRSIRNQ KKES
//
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