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Database: UniProt
Entry: M5W636_PRUPE
LinkDB: M5W636_PRUPE
Original site: M5W636_PRUPE 
ID   M5W636_PRUPE            Unreviewed;       378 AA.
AC   M5W636;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000256|ARBA:ARBA00013211};
DE            EC=2.3.1.51 {ECO:0000256|ARBA:ARBA00013211};
GN   ORFNames=PRUPE_8G103400 {ECO:0000313|EMBL:ONH91281.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONH91281.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONH91281.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
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|ARBA:ARBA00001141};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004728}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   EMBL; CM007658; ONH91281.1; -; Genomic_DNA.
DR   RefSeq; XP_007201056.1; XM_007200994.1.
DR   AlphaFoldDB; M5W636; -.
DR   STRING; 3760.M5W636; -.
DR   EnsemblPlants; ONH91281; ONH91281; PRUPE_8G103400.
DR   GeneID; 18766882; -.
DR   Gramene; ONH91281; ONH91281; PRUPE_8G103400.
DR   eggNOG; KOG1505; Eukaryota.
DR   OMA; GTHAKKV; -.
DR   OrthoDB; 2906776at2759; -.
DR   UniPathway; UPA00557; UER00613.
DR   Proteomes; UP000006882; Chromosome g8.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR   InterPro; IPR032098; Acyltransf_C.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10983:SF76; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE EPSILON; 1.
DR   PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF16076; Acyltransf_C; 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|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          98..220
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   378 AA;  43238 MW;  64454D4337A80F84 CRC64;
     MEVQKPSNDA MKHLPLTPLR AIRGVVCLLI LVSTAFMMLV YFGFLGAVII RLFSIHYSRR
     VTSFFFGAWL ALWPFLFEKI NKTKVIFSGE TVPDGERILL ISNHRTEVDW MYLWDLALRK
     GRQGYIKYIL KSSLMKLPLF GWSFHILEFI SVERKWEVDE LNMRRMLSSL KDPQDSLWLA
     LFPEGTDFTE QKCIRSQKYA AENGLPVLKH VLLPKTKGFS ACLEELRGSL DAVYDVTIGY
     KPSCPTFFDN ASGVNPSEVH MHVQRIPLDN IPTSEDEVTT WLMNRFHLKD QLLSDFDSQG
     HFPHEGSEGD LSTLRCLVNL VAVIVLTGTC AYLTIFSSIW FKIYVSLVCA YLTAATIFNI
     RPLPLVSLVK AWFKCKSS
//
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