ID I2GWV3_TETBL Unreviewed; 266 AA.
AC I2GWV3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 Name=TBLA0A08150 {ECO:0000313|EMBL:CCH58605.1};
GN ORFNames=TBLA_0A08150 {ECO:0000313|EMBL:CCH58605.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH58605.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH58605.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE806316; CCH58605.1; -; Genomic_DNA.
DR RefSeq; XP_004178124.1; XM_004178076.1.
DR AlphaFoldDB; I2GWV3; -.
DR STRING; 1071380.I2GWV3; -.
DR GeneID; 14493456; -.
DR KEGG; tbl:TBLA_0A08150; -.
DR eggNOG; KOG2848; Eukaryota.
DR HOGENOM; CLU_027938_10_0_1; -.
DR InParanoid; I2GWV3; -.
DR OMA; CKHQSAW; -.
DR OrthoDB; 209232at2759; -.
DR Proteomes; UP000002866; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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 Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW Transferase {ECO:0000256|RuleBase:RU361267}.
FT DOMAIN 74..191
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 266 AA; 30023 MW; 0B392272FB71A150 CRC64;
MGNFKYYFRT VTLSLLLLVS ALYGTIASIV LNVIGKKHLS QWATARFYYN LVKYVLGIEI
RVINEDILTK HVPCIFVSNH QSTLDILMLG RMFPKGCTVT AKKSLKYIPF LGWFMALSGT
YFLERSSREK SVATLNKGLE DVKRKKQSLW IFPEGTRSYS QDLIIAPFKK GAFHLAQQGK
LPIVPIVVSN TSTVVASKWK VFNRGEIVVK VLPPMATDQL SSEGVSKFST EIHDLMVNEL
QTIGYSKVIN DTNLPPHAEK YLLNKN
//
