ID A8Q6M5_MALGO Unreviewed; 301 AA.
AC A8Q6M5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=MGL_3009 {ECO:0000313|EMBL:EDP42809.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP42809.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP42809.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP42809.1}.
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DR EMBL; AAYY01000010; EDP42809.1; -; Genomic_DNA.
DR RefSeq; XP_001730023.1; XM_001729971.1.
DR AlphaFoldDB; A8Q6M5; -.
DR STRING; 425265.A8Q6M5; -.
DR GeneID; 5854330; -.
DR KEGG; mgl:MGL_3009; -.
DR VEuPathDB; FungiDB:MGL_3009; -.
DR InParanoid; A8Q6M5; -.
DR OMA; KKSLVWI; -.
DR OrthoDB; 209232at2759; -.
DR Proteomes; UP000008837; 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; 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:UP000008837};
KW Transferase {ECO:0000256|RuleBase:RU361267};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..216
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 277..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 33653 MW; 5D005FEE92501BD7 CRC64;
MGKLVHGVST VGAVSFLLLT LASRRSQRAR FYLNSILCVI SMALSSSIGV VCGLVLSLFP
GKRFNVNYIV ARSFHFFMKP LIGMYVEVEG EEHLKRRPAI MVGNHQSSID TLYLGRMFPV
NSIIMAKKEL KWVPFLGQFM MLSGSAFIDR KSRASAIKTM NATGEHMRKN NLMLFVFPEG
TRSNLSTPDM LPFKKGAFHL AVQTQLPIIP MVCENYHRLF DSKTRFEPGK IRLKILPPIE
TTGMTEKDVD MLCNTVREKM LSQLLSYAND VKQQKIEASS DSSGTSSSVN TRALPGLSAR
F
//
