ID Q87TX7_PSESM Unreviewed; 206 AA.
AC Q87TX7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Acyltransferase, putative {ECO:0000313|EMBL:AAO58959.1};
GN OrderedLocusNames=PSPTO_5540 {ECO:0000313|EMBL:AAO58959.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO58959.1, ECO:0000313|Proteomes:UP000002515};
RN [1] {ECO:0000313|EMBL:AAO58959.1, ECO:0000313|Proteomes:UP000002515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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DR EMBL; AE016853; AAO58959.1; -; Genomic_DNA.
DR RefSeq; NP_795264.1; NC_004578.1.
DR RefSeq; WP_011105553.1; NC_004578.1.
DR AlphaFoldDB; Q87TX7; -.
DR STRING; 223283.PSPTO_5540; -.
DR GeneID; 1187232; -.
DR KEGG; pst:PSPTO_5540; -.
DR PATRIC; fig|223283.9.peg.5675; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_8_1_6; -.
DR OrthoDB; 9808424at2; -.
DR PhylomeDB; Q87TX7; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:AAO58959.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002515};
KW Transferase {ECO:0000313|EMBL:AAO58959.1}.
FT DOMAIN 34..155
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 206 AA; 23023 MW; AB89DE9DE11BAE74 CRC64;
MFEPLVATII TAGARSITGA RSLWLGCTPE LRQRIYFANH SSHGDFVLLW ASLPPALRKT
ARPVAGADYW QTSPLRRYII NRVFNGVLVD RKRSTPESNP LQPMLEALEN GDSLIFFPEG
TRNPEDGLLP FKSGLYHLAQ SYPQVDLVPV WIANLNRVMP KGRMLPLPLL CTTSFGAPLR
LDSEESKEQF LTRSRDALLA LAPEPL
//
