ID   PLSX_DESVV              Reviewed;         345 AA.
AC   A1VEK0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Dvul_1849;
OS   Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=391774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP4;
RX   PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA   Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA   He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA   Stahl D.A.;
RT   "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT   plasticity.";
RL   Environ. Microbiol. 11:2244-2252(2009).
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}.
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DR   EMBL; CP000527; ABM28866.1; -; Genomic_DNA.
DR   RefSeq; WP_010938504.1; NC_008751.1.
DR   AlphaFoldDB; A1VEK0; -.
DR   SMR; A1VEK0; -.
DR   EnsemblBacteria; ABM28866; ABM28866; Dvul_1849.
DR   KEGG; dvl:Dvul_1849; -.
DR   HOGENOM; CLU_039379_1_1_7; -.
DR   OMA; HGKSNAR; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000009173; Chromosome.
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..345
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_1000001754"
SQ   SEQUENCE   345 AA;  36895 MW;  8FD4DBAE1F95CECD CRC64;
     MNSTIIAVDA MGGDFGPSVV VPGAVDAARE RGLKVLLVGD RQKVEEELAR IPLDGVEVEV
     VHASEVAGMD EKPSDILRRK KDASIQVVCR LVRDGHAHGI VSAGHSGASV ACGMFIMGRV
     PGVERPALAS VMPTEKQPIV LLDVGANVDC KPHHLFQFGL MANAFARDLL GYETPRIGLL
     SIGEEEGKGN TLVKEAYELF KLAQNINFVG NVEGRDLFTG EVDVVVCDGF VGNVALKLSE
     GLSSSMSRVL KRELLSGFLP KLGTLLARSA FKRFARVVDY AEYGGAPLLG LQSIAIVCHG
     KSNAKAIKSA VNMAATFVEK KTNERVVQAI CANEELTRYG KAVRQ