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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)

 A0A161X8U4_9RHOB        Unreviewed;       205 AA.
A0A161X8U4;
06-JUL-2016, integrated into UniProtKB/TrEMBL.
06-JUL-2016, sequence version 1.
05-DEC-2018, entry version 12.
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_1 {ECO:0000313|EMBL:KZL06706.1};
Synonyms=plsY {ECO:0000256|HAMAP-Rule:MF_01043};
ORFNames=PsAD2_04219 {ECO:0000313|EMBL:KZL06706.1};
Pseudovibrio axinellae.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Pseudovibrio.
NCBI_TaxID=989403 {ECO:0000313|EMBL:KZL06706.1, ECO:0000313|Proteomes:UP000076577};
[1] {ECO:0000313|EMBL:KZL06706.1, ECO:0000313|Proteomes:UP000076577}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ad2 {ECO:0000313|EMBL:KZL06706.1,
ECO:0000313|Proteomes:UP000076577};
PubMed=27065959; DOI=10.3389/fmicb.2016.00387;
Romano S., Fernandez-Guerra A., Reen F.J., Glockner F.O.,
Crowley S.P., O'Sullivan O., Cotter P.D., Adams C., Dobson A.D.,
O'Gara F.;
"Comparative Genomic Analysis Reveals a Diverse Repertoire of Genes
Involved in Prokaryote-Eukaryote Interactions within the Pseudovibrio
Genus.";
Front. Microbiol. 7:387-387(2016).
-!- 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:
Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-
sn-glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970,
ChEBI:CHEBI:59918; EC=2.3.1.n3; Evidence={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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KZL06706.1}.
-----------------------------------------------------------------------
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EMBL; LMCB01000139; KZL06706.1; -; Genomic_DNA.
RefSeq; WP_068010369.1; NZ_LMCB01000139.1.
EnsemblBacteria; KZL06706; KZL06706; PsAD2_04219.
PATRIC; fig|989403.3.peg.4611; -.
UniPathway; UPA00085; -.
Proteomes; UP000076577; Unassembled WGS sequence.
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;
Acyltransferase {ECO:0000313|EMBL:KZL06706.1};
Cell membrane {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702469};
Complete proteome {ECO:0000313|Proteomes:UP000076577};
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};
Reference proteome {ECO:0000313|Proteomes:UP000076577};
Transferase {ECO:0000313|EMBL:KZL06706.1};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702429};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|SAAS:SAAS00702429}.
TRANSMEM 12 33 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
TRANSMEM 90 108 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
TRANSMEM 120 141 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
TRANSMEM 147 166 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
SEQUENCE 205 AA; 22035 MW; 682616174241AC70 CRC64;
MPEPISWSFD LPYYLAALAF GYLLGSIPFG LLFTKMAGHG DIRNIGSGNI GTTNVLRTGS
KKLAALTLLC DALKGTTAVV LIGFFMGNEA ALIAGLGAFL GHLFPVWLKF KGGKGVATYI
GILLGIFWPV GIIFIVIWIA TAYITKFSSL SALVASLVTP FILMAFDQWQ IAQMMGLLSV
LLWAKHHENI ARLIKGKESK IGSKG


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