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-MAR-2009, entry version 47.
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; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACCAD clade; Panicoideae; Andropogoneae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ENZYME ACTIVITY.
RC   STRAIN=cv. Black Mexican Sweet; TISSUE=Endosperm;
RX   MEDLINE=95035993; 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-
RT   acyl sn-glycerol-3-phosphate acyltransferase mutant of E.coli and
RT   encodes a protein which has similarities to other acyltransferases.";
RL   Plant Mol. Biol. 26:211-223(1994).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC       acid by incorporating acyl moiety at the 2 position.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family.
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DR   EMBL; Z29518; CAA82638.1; -; mRNA.
DR   PIR; S52645; S52645.
DR   RefSeq; NP_001105919.1; -.
DR   UniGene; Zm.95920; -.
DR   GeneID; 732844; -.
DR   Gramene; Q41745; -.
DR   MaizeGDB; 98837; -.
DR   BRENDA; 2.3.1.51; 289.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferas...; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002123; Acyltransferase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Membrane; Phospholipid biosynthesis; Transferase;
KW   Transmembrane.
FT   CHAIN         1    374       1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase PLS1.
FT                                /FTId=PRO_0000208188.
FT   TRANSMEM     15     37       Potential.
FT   TRANSMEM     48     68       Potential.
FT   TRANSMEM    121    141       Potential.
FT   TRANSMEM    305    325       Potential.
FT   TRANSMEM    335    355       Potential.
FT   MOTIF        92     97       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
//