PLSX_HAEDU
ID PLSX_HAEDU Reviewed; 343 AA.
AC Q7VN19;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=HD_0773;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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}.
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DR EMBL; AE017143; AAP95678.1; -; Genomic_DNA.
DR RefSeq; WP_010944728.1; NC_002940.2.
DR AlphaFoldDB; Q7VN19; -.
DR SMR; Q7VN19; -.
DR STRING; 233412.HD_0773; -.
DR EnsemblBacteria; AAP95678; AAP95678; HD_0773.
DR KEGG; hdu:HD_0773; -.
DR eggNOG; COG0416; Bacteria.
DR HOGENOM; CLU_039379_1_0_6; -.
DR OMA; HGKSNAR; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000001022; 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; Reference proteome; Transferase.
FT CHAIN 1..343
FT /note="Phosphate acyltransferase"
FT /id="PRO_0000189885"
SQ SEQUENCE 343 AA; 37580 MW; 9004E5BBC8387DFD CRC64;
MNRLTLALDV MGGDFGPRVT IPALSLALAQ QPMLSFVLFG DQYHAIPLLH SLPAEQQQRI
RFVHTSRIVD PHVPVRQALR QSKGSSMRLA IEAVVAGEAQ ACVSGGNTGV LMGLAKWFVE
PLVGIDRPAL ASLIPALNGQ ASVMLDLGAN VEADSKLLLQ FAEMGNIFAQ SILSLAQPRL
ALLNIGTEEV KGRYAIQQAH HVLKNRADLH YIGFIESDKL MNHLADVIVC DGFCGNIALK
AVEGVASHFL ALFKQPKRSF FVDWLSSWWG RLLYHRVYRA LQRVNPERHN GATLLGLSSV
VVKSHGSAGV NAYFYAINHA IEQIQNRIPV KISAGLQKLH QNL