PLSB_PSEPW
ID PLSB_PSEPW Reviewed; 828 AA.
AC B1JBS6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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};
GN OrderedLocusNames=PputW619_4098;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000949; ACA74578.1; -; Genomic_DNA.
DR RefSeq; WP_012315915.1; NC_010501.1.
DR AlphaFoldDB; B1JBS6; -.
DR SMR; B1JBS6; -.
DR STRING; 390235.PputW619_4098; -.
DR PRIDE; B1JBS6; -.
DR EnsemblBacteria; ACA74578; ACA74578; PputW619_4098.
DR KEGG; ppw:PputW619_4098; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR UniPathway; UPA00557; UER00612.
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; Transferase.
FT CHAIN 1..828
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000123088"
FT MOTIF 309..314
FT /note="HXXXXD motif"
SQ SEQUENCE 828 AA; 93727 MW; 83FF9110B0FF41CF CRC64;
MTRSPLRRLI FGALRRLLYL WVRSETINQS AMSLQLDRSR PVFYALPSPS LTDLAVLDHE
CTKAGLPRPV LPVAVGTLHE PAGFFYLTPD PDWLGRHDKR GAPPTLERVI AAVSQHAEED
AQIIPVSVFW GQTPASESSP WKLLFADSWA VTGRLRRLLT ILILGRKTRV QFSAPIQVRD
LVQHNKGHER TVRMAQRLMR VHFRNLKTAV IGPDISHRRN LVKGLVHAPL VRQAINEQAQ
RENIPVAKAE AQALRYGNEI ASDYTYTAIR FLEVVLSWFW NKIYDGIKVN HIEQVQGIAP
GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVIGGLLRR GGAFFMRRTF
KGNPLYTAVF NEYLHTLFTK GFPVEYFVEG GRSRTGRMLQ PRTGMLAITL RSFLRSSRTP
IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESIFDIFKVI GALKQRFGQV YVNFGEPIRL
AGFLDQQQPG WREQALGPQF RPAWLNETTT RLGETVARHL NEAAAVNPVN LVALALLSTS
RLALDESALT RVLDLYLTLL RKVPYSQHTT LPEGDGQALI EHVRGMNLLA EQKDALGRIL
YLDEANAVLM TYYRNNVLHI FALPALLASF FHSSSRMSRD LLGQYVHALY PYLQAELFLR
WAPEQLDEVI DQWLAALVEQ GLLRRENDLY VRPAPSSRQF VLLTLLARTI TQTLQRFYMA
TSLLLNSGQN TLSAEALEDL CVMMAQRLSI LHGLNAPEFF DKTLFRHFIQ TLVEQGVLRP
DGNGKLGYHD KLGELAEGVA KRVLSAELRL SIRQVALHRE HALEASIL
