PLSB_PSESM
ID PLSB_PSESM Reviewed; 833 AA.
AC Q886Q7;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00393};
DE Short=GPAT {ECO:0000255|HAMAP-Rule:MF_00393};
DE EC=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_00393};
GN Name=plsB {ECO:0000255|HAMAP-Rule:MF_00393}; OrderedLocusNames=PSPTO_1520;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
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.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA 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 -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00393};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000255|HAMAP-Rule:MF_00393}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00393}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00393}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00393}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00393}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000255|HAMAP-
CC Rule:MF_00393}.
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DR EMBL; AE016853; AAO55040.1; -; Genomic_DNA.
DR RefSeq; NP_791345.1; NC_004578.1.
DR RefSeq; WP_007245401.1; NC_004578.1.
DR AlphaFoldDB; Q886Q7; -.
DR SMR; Q886Q7; -.
DR STRING; 223283.PSPTO_1520; -.
DR EnsemblBacteria; AAO55040; AAO55040; PSPTO_1520.
DR GeneID; 1183157; -.
DR KEGG; pst:PSPTO_1520; -.
DR PATRIC; fig|223283.9.peg.1543; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR PhylomeDB; Q886Q7; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR045520; GPAT_C.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500064; GPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
DR TIGRFAMs; TIGR03703; plsB; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..833
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195230"
FT MOTIF 310..315
FT /note="HXXXXD motif"
SQ SEQUENCE 833 AA; 94878 MW; 957B736D1FA077A2 CRC64;
MTRSPFRRLV FGTLRRLLYL WVRSETINQS SFTLNLDRSR PVFYALQSPS ISDLAVIDTE
CRKAGLPRPV LSVAVGNLIE PSAYFYLTPA PDWLGRQDKR GAPPTLERLV AAVSQNPGED
AQIIPVSVFW GQSPDHESSA WKLLFADSWA VTGRLRRLVS ILILGRKTRV QFSAPIHMRE
LVDQNKGHEL TLRMSQRLLR THFRNLKSAV IGPDVSHRRT VVKGLLDEPL VKQAIIEEAE
RENITQEKAR ERALSYGNEI ASDYTYSVIR FMEVVLSWFW NKIYDGIKVS HIEGVQEIAP
GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVVGSLLRR GGAFFMRRTF
KGSPLYTAVF TEYLHTLFTK GFPVEYFVEG GRSRTGRMLQ PKTGMLAITL RSFLRNSRMP
IVFIPVYIGY ERVLEGRTYL GELRGATKKK ESIFDIFKVI GALKQRFGQV SVNFGEPIRL
AEFLDGEQPD WREQELAPQF RPDWLSETTH RLGERVAQHL NEAAAVNPMN LVAITLLSTQ
KLALDDQAME RVLDLYLTLL RAVPYSPHTT LPEGNGRSLI EHVKGMDLLA EQKDALGKIL
YLNEQNAVLM TYYRNNVLHI FALPSLLASF FQSSSRMSRE QILRYTHALY PYLQSELFIR
WPLSELDEVV DQWLAAFVEQ GLLRFRNDAY VRPEPSSREF VLLTLLSRAI AQTLQRFYMA
IALLLNSGPN TLNPEELEDL CTVMAQRLSI LHGLNAPEFF DKSLFRHFIQ TLLDLRVLRK
DRAGKLSYHP MLGELAEGAA KRVLPAEIRL SIRQVALHSN EEEQNAGNES GAA
