PLSY_VIBVU
ID PLSY_VIBVU Reviewed; 203 AA.
AC P59257;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=GPAT {ECO:0000255|HAMAP-Rule:MF_01043};
DE EC=2.3.1.275 {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Lysophosphatidic acid synthase {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=LPA synthase {ECO:0000255|HAMAP-Rule:MF_01043};
GN Name=plsY {ECO:0000255|HAMAP-Rule:MF_01043}; OrderedLocusNames=VV1_0626;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate
CC (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic
CC acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor,
CC but not acyl-CoA or acyl-ACP. {ECO:0000255|HAMAP-Rule:MF_01043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:59918; EC=2.3.1.275; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01043};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01043}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
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DR EMBL; AE016795; AAO09140.1; -; Genomic_DNA.
DR RefSeq; WP_011078709.1; NC_004459.3.
DR AlphaFoldDB; P59257; -.
DR SMR; P59257; -.
DR EnsemblBacteria; AAO09140; AAO09140; VV1_0626.
DR KEGG; vvu:VV1_0626; -.
DR HOGENOM; CLU_081254_0_2_6; -.
DR OMA; WRHRGNL; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000002275; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01043; PlsY; 1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR PANTHER; PTHR30309; PTHR30309; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR SMART; SM01207; G3P_acyltransf; 1.
DR TIGRFAMs; TIGR00023; TIGR00023; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..203
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188488"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ SEQUENCE 203 AA; 21781 MW; F76DA1CAB170B8AA CRC64;
MDAMAVTMTI IAYLLGSISS AVLICRVLRL PDPRGVGSNN PGATNVLRIG GKGAAAAVLL
CDMLKGTIPV WSGYYLGIEP VLLGVIAIAA CLGHMYPLFF HFQGGKGVAT ALGAIAPIGL
DLTGMIMATW LLVAILFRYS SLAALVTVLL APMYTWMIKP QYTLPVGMLC CLIVLRHHQN
IRRLFTGEEP KIGEKKLQMP KSQ
