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Glycerol-3-phosphate acyltransferase (Acyl-PO4 G3P acyltransferase) (Acyl-phosphate--glycerol-3-phosphate acyltransferase) (G3P acyltransferase) (GPAT) (EC 2.3.1.n3) (Lysophosphatidic acid synthase) (LPA synthase)

 Q1PJI1_PROMR            Unreviewed;       196 AA.
Q1PJI1;
16-MAY-2006, integrated into UniProtKB/TrEMBL.
16-MAY-2006, sequence version 1.
27-SEP-2017, entry version 41.
RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
AltName: Full=G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
Short=GPAT {ECO:0000256|HAMAP-Rule:MF_01043};
EC=2.3.1.n3 {ECO:0000256|HAMAP-Rule:MF_01043};
AltName: Full=Lysophosphatidic acid synthase {ECO:0000256|HAMAP-Rule:MF_01043};
Short=LPA synthase {ECO:0000256|HAMAP-Rule:MF_01043};
Name=plsY {ECO:0000256|HAMAP-Rule:MF_01043};
ORFNames=HOT0M-1A11_0006 {ECO:0000313|EMBL:ABE11399.1};
uncultured Prochlorococcus marinus clone HOT0M-1A11.
Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
Prochlorococcus.
NCBI_TaxID=379386 {ECO:0000313|EMBL:ABE11399.1};
[1] {ECO:0000313|EMBL:ABE11399.1}
NUCLEOTIDE SEQUENCE.
PubMed=16556843; DOI=10.1126/science.1122050;
Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
Delong E.F., Chisholm S.W.;
"Genomic islands and the ecology and evolution of Prochlorococcus.";
Science 311:1768-1770(2006).
[2] {ECO:0000313|EMBL:ABE11399.1}
NUCLEOTIDE SEQUENCE.
US DOE Joint Genome Institute (JGI);
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Richardson P.;
"Sequencing of the draft fosmids and assembly of Prochlorococcus
marinus environmental genome fragment.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-
phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form
lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate
as fatty acyl donor, but not acyl-CoA or acyl-ACP.
{ECO:0000256|HAMAP-Rule:MF_01043}.
-!- CATALYTIC ACTIVITY: Acyl-phosphate + sn-glycerol 3-phosphate = 1-
acyl-sn-glycerol 3-phosphate + phosphate. {ECO:0000256|HAMAP-
Rule:MF_01043}.
-!- PATHWAY: Lipid metabolism; phospholipid metabolism.
{ECO:0000256|HAMAP-Rule:MF_01043, ECO:0000256|SAAS:SAAS00702448}.
-!- SUBUNIT: Probably interacts with PlsX. {ECO:0000256|HAMAP-
Rule:MF_01043, ECO:0000256|SAAS:SAAS00702495}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
Rule:MF_01043}; Multi-pass membrane protein {ECO:0000256|HAMAP-
Rule:MF_01043}.
-!- SIMILARITY: Belongs to the PlsY family. {ECO:0000256|HAMAP-
Rule:MF_01043, ECO:0000256|SAAS:SAAS00702497}.
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EMBL; DQ366734; ABE11399.1; -; Genomic_DNA.
UniPathway; UPA00085; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_01043; PlsY; 1.
InterPro; IPR003811; G3P_acylTferase_PlsY.
PANTHER; PTHR30309; PTHR30309; 1.
Pfam; PF02660; G3P_acyltransf; 1.
SMART; SM01207; G3P_acyltransf; 1.
TIGRFAMs; TIGR00023; TIGR00023; 1.
3: Inferred from homology;
Cell membrane {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702469};
Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702501};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702501};
Membrane {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702429, ECO:0000256|SAAS:SAAS00702469};
Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702501};
Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702501};
Transferase {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702475};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702429};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702429}.
TRANSMEM 77 96 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
TRANSMEM 108 129 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
TRANSMEM 136 154 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
TRANSMEM 160 176 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
SEQUENCE 196 AA; 21482 MW; 153C7835EB4A2043 CRC64;
MNILIIFISY LLGSLPTGFL IGKYLKNIDL RTIGSGSTGA TNVLRNVGKW PALFVFIIDV
GKGLIAVKIA QFYTDQGLIE VIAGISAISG HIWPIWLRGK GGKAVATGLG MFLALSWKVG
LASLGIFLIV LTKTKFVSLS SISAAILLPI FMFFYLGNFM HSYFFISLIV SLLVIWKHRS
NITRLLKGEE SKINQN


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