ID   LPAT_MAIZE              Reviewed;         374 AA.
AC   Q41745;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase PLS1;
DE            EC=2.3.1.51;
DE   AltName: Full=Phospholipid synthesis protein 1;
GN   Name=PLS1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ENZYME ACTIVITY.
RC   STRAIN=cv. Black Mexican Sweet; TISSUE=Endosperm;
RX   PubMed=7948871; DOI=10.1007/bf00039533;
RA   Brown A.P., Coleman J., Tommey A.M., Watson M.D., Slabas A.R.;
RT   "Isolation and characterization of a maize cDNA that complements a 1-acyl
RT   sn-glycerol-3-phosphate acyltransferase mutant of E.coli and encodes a
RT   protein which has similarities to other acyltransferases.";
RL   Plant Mol. Biol. 26:211-223(1994).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating acyl moiety at the 2 position.
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:0000269|PubMed:7948871};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000305}.
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DR   EMBL; Z29518; CAA82638.1; -; mRNA.
DR   PIR; S52645; S52645.
DR   RefSeq; NP_001105919.1; NM_001112449.1.
DR   AlphaFoldDB; Q41745; -.
DR   STRING; 4577.GRMZM2G037104_P01; -.
DR   PaxDb; Q41745; -.
DR   PRIDE; Q41745; -.
DR   EnsemblPlants; Zm00001eb115270_T001; Zm00001eb115270_P001; Zm00001eb115270.
DR   GeneID; 732844; -.
DR   Gramene; Zm00001eb115270_T001; Zm00001eb115270_P001; Zm00001eb115270.
DR   KEGG; zma:732844; -.
DR   MaizeGDB; 98837; -.
DR   eggNOG; KOG1505; Eukaryota.
DR   OMA; IAQWCIN; -.
DR   OrthoDB; 959325at2759; -.
DR   UniPathway; UPA00557; UER00613.
DR   Proteomes; UP000007305; Chromosome 2.
DR   ExpressionAtlas; Q41745; baseline and differential.
DR   Genevisible; Q41745; ZM.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR032098; Acyltransf_C.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF16076; Acyltransf_C; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..374
FT                   /note="1-acyl-sn-glycerol-3-phosphate acyltransferase PLS1"
FT                   /id="PRO_0000208188"
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           92..97
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   374 AA;  42571 MW;  F1F5492CAFF24F93 CRC64;
     MAIPLVLVVL PLGLLFLLSG LIVNAIQAVL FVTIRPFSKS FYRRINRFLA ELLWLQLVWV
     VDWWAGVKVQ LHADEETYRS MGKEHALIIS NHRSDIDWLI GWILAQRSGC LGSTLAVMKK
     SSKFLPVIGW SMWFAEYLFL ERSWAKDEKT LKWGLQRLKD FPRPFWLALF VEGTRFTPAK
     LLAAQEYAAS QGLPAPRNVL IPRTKGFVSA VSIMRDFVPA IYDTTVIVPK DSPQPTMLRI
     LKGQSSVIHV RMKRHAMSEM PKSDEDVSKW CKDIFVAKDA LLDKHLATGT FDEEIRPIGR
     PVKSLLVTLF WSCLLLFGAI EFFKWTQLLS TWRGVAFTAA GMALVTGVMH VFIMFSQAER
     SSSARAARNR VKKE