PLSX_PSEMY
ID PLSX_PSEMY Reviewed; 336 AA.
AC A4XSS4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE EC=2.3.1.274 {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
GN Name=plsX {ECO:0000255|HAMAP-Rule:MF_00019}; OrderedLocusNames=Pmen_1626;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible formation of acyl-phosphate (acyl-
CC PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme
CC utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
CC {ECO:0000255|HAMAP-Rule:MF_00019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-
CC [ACP]; Xref=Rhea:RHEA:42292, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:14125, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:138651; EC=2.3.1.274; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00019};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SUBUNIT: Homodimer. Probably interacts with PlsY. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00019}.
CC Note=Associated with the membrane possibly through PlsY.
CC {ECO:0000255|HAMAP-Rule:MF_00019}.
CC -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABP84390.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000680; ABP84390.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A4XSS4; -.
DR SMR; A4XSS4; -.
DR STRING; 399739.Pmen_1626; -.
DR EnsemblBacteria; ABP84390; ABP84390; Pmen_1626.
DR KEGG; pmy:Pmen_1626; -.
DR eggNOG; COG0416; Bacteria.
DR HOGENOM; CLU_039379_1_0_6; -.
DR UniPathway; UPA00085; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043811; F:phosphate:acyl-[acyl carrier protein] acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR HAMAP; MF_00019; PlsX; 1.
DR InterPro; IPR003664; FA_synthesis.
DR InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR PANTHER; PTHR30100; PTHR30100; 1.
DR Pfam; PF02504; FA_synthesis; 1.
DR PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR TIGRFAMs; TIGR00182; plsX; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase.
FT CHAIN 1..336
FT /note="Phosphate acyltransferase"
FT /id="PRO_0000329254"
SQ SEQUENCE 336 AA; 35714 MW; 9C89366E91878F01 CRC64;
MSASIIAIDA MGGDFGPHCI VPACISALAE FPSLHLALVG QAPLIEEQLA RQSGVDRSRL
QVHHASEVIA MDERPAQALR GKPDASMRVA LELVRQRQAH ACVSAGNTGA LMALSRYVLK
TLPGIDRPAM VSPIPTERGH CYLLDLGANV DCSAEHLYQF AIMGAVAAET LGVARPRVAL
LNVGTEDIKG NQQVKLAASL LLQARGLNFI GYIEGDGVYR GEADVVVCDG FVGNILLKAS
EGLAKMITGR VETLFNEGLF AQAVGALAMP LLRRLKADLA PARHNGASFL GLQGIVVKSH
GAAGQESFQS AIRCALREVQ ENLPQRLHGR LEDLLL