PLSX_TRIV2
ID PLSX_TRIV2 Reviewed; 342 AA.
AC Q3M9J5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Ava_2728;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA22341.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3M9J5; -.
DR SMR; Q3M9J5; -.
DR STRING; 240292.Ava_2728; -.
DR EnsemblBacteria; ABA22341; ABA22341; Ava_2728.
DR KEGG; ava:Ava_2728; -.
DR eggNOG; COG0416; Bacteria.
DR HOGENOM; CLU_039379_1_1_3; -.
DR OMA; HGKSNAR; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000002533; 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..342
FT /note="Phosphate acyltransferase"
FT /id="PRO_1000001716"
SQ SEQUENCE 342 AA; 36329 MW; C913B3C458E7FE06 CRC64;
MGSTCVRIAI DAMGGDHAPN EIVAGAVRAS EELGVKVLLV GDPQQIASAL PPKTNLERVE
IVPAEEAIAM DEEPLNAVRR KRKASINVAM DLVKREQADA IFSAGHSGAA MASALLRLGR
LPGVDRPAIG TVFPTIKAGK PVLILDVGAN VDCRPKFLEQ FAVIGSIYSQ YVLGTGEPPK
VGLLNIGEED TKGNELALRT HQLLKDNPNI NFIGNAEGRD VLSGEFDVIV CDGFVGNILL
KFAEAIGGVI LQILREELPQ GLHGQIGTAI LKPNLTRIKQ RMDHAEHGGA LLLGVSGVCL
IGHGSSQAPS VFNAIRMAKE AVDNQVMQQL QSQYEILHSA SD
