PLSX_ONYPE
ID PLSX_ONYPE Reviewed; 366 AA.
AC Q6YPW8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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}; Synonyms=pam607;
GN OrderedLocusNames=PAM_607;
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=262768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M;
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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; AP006628; BAD04692.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YPW8; -.
DR SMR; Q6YPW8; -.
DR STRING; 262768.PAM_607; -.
DR EnsemblBacteria; BAD04692; BAD04692; PAM_607.
DR KEGG; poy:PAM_607; -.
DR eggNOG; COG0416; Bacteria.
DR HOGENOM; CLU_039379_1_1_14; -.
DR OMA; HGKSNAR; -.
DR OrthoDB; 631784at2; -.
DR BioCyc; OYEL262768:G1G26-733-MON; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000002523; 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..366
FT /note="Phosphate acyltransferase"
FT /id="PRO_1000201894"
FT REGION 334..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 40424 MW; 4B8AFDC74191A0AE CRC64;
MIKIAIDVMG GDFAPLEIVK GTLLALNKNK EIHVVLYGNQ KLITPLIEKT PFFGNNQITI
KHTPYFLRSA DKNIRDQLKA TPNASLFLAL EAAKQDEVQG VVSAGATQTL VLASHLILKK
MPLMQRIAIA PMFNSFDNRT RILLDAGANT ELKPQHLHTF ANYATIIAKE ILEIPNPQIK
LLNIGTEPTK GRALELETYQ LLSQDSNLNF GGNEEPQNLL TTSADILLSD GFTANIALKT
YEGTMLNFMN HFKTILTKNL IKKMATKTLF QKPLQQLKNQ LDPRQIGGAM LLGLNKIVIK
AHGSSQAYAF CQAILQAQKL IKAQVNQKIA HSLESAKNKE TQSKQASTKN TAPKTSETTK
ESQQSL