PLSX_PARMW
ID PLSX_PARMW Reviewed; 428 AA.
AC Q7U428;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Phosphate acyltransferase;
DE EC=2.3.1.274;
DE AltName: Full=Acyl-ACP phosphotransacylase;
DE AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase;
DE AltName: Full=Phosphate-acyl-ACP acyltransferase;
GN Name=plsX; OrderedLocusNames=SYNW2247;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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 (By
CC similarity). {ECO:0000250}.
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;
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBUNIT: Homodimer. Probably interacts with PlsY (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated with the
CC membrane possibly through PlsY. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000305}.
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DR EMBL; BX569695; CAE08762.1; -; Genomic_DNA.
DR RefSeq; WP_011129100.1; NC_005070.1.
DR AlphaFoldDB; Q7U428; -.
DR SMR; Q7U428; -.
DR STRING; 84588.SYNW2247; -.
DR EnsemblBacteria; CAE08762; CAE08762; SYNW2247.
DR KEGG; syw:SYNW2247; -.
DR eggNOG; COG0416; Bacteria.
DR HOGENOM; CLU_039379_0_0_3; -.
DR OMA; HGKSNAR; -.
DR OrthoDB; 631784at2; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000001422; 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 TIGRFAMs; TIGR00182; plsX; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase.
FT CHAIN 1..428
FT /note="Phosphate acyltransferase"
FT /id="PRO_0000189955"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 45589 MW; 7267CAB6055ED107 CRC64;
MPPKDPDSSR TPESRSKSNR PRAIRRLVIW YRRNAAVTSL VDTATSSASA AGTVAGTVAN
SMLQPLVFDP LRWLQGNTDD EEIQEADRLW VAVDGMGGDH APGPILEGCL EAIERLPLKI
RFVGETDKVL EAADALGLSE RLAQAQAADH LDLVASGPSI GMDDEATAVR RKRDASINLA
MDLVKKGQAL AVYSAGNSGA MMASAIFRLG RLKGIDRPAI GALFPTKDPG QPVLVLDVGA
NMDCKPAYLH QFALLGNIYS RDVLQVEQPR IGLLNIGEED CKGNDLALKT HALLRDERRL
HFAGNCEGRD VLSGAFDVVV CDGFTGNVLL KFLESVGSVL LGVLRAELPR GRRGKVGSAF
LRSNLRRIKK RLDHAEHGGA LLLGVNGVAV IGHGSSKALS VVSALRIAHS AASHGVMEDL
AALQSGCD
