PLSB_PSEAE
ID PLSB_PSEAE Reviewed; 834 AA.
AC Q9HXW7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glycerol-3-phosphate acyltransferase;
DE Short=GPAT;
DE EC=2.3.1.15;
GN Name=plsB; OrderedLocusNames=PA3673;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; AE004091; AAG07061.1; -; Genomic_DNA.
DR PIR; F83185; F83185.
DR RefSeq; NP_252363.1; NC_002516.2.
DR RefSeq; WP_003113856.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXW7; -.
DR STRING; 287.DR97_4204; -.
DR PaxDb; Q9HXW7; -.
DR PRIDE; Q9HXW7; -.
DR EnsemblBacteria; AAG07061; AAG07061; PA3673.
DR GeneID; 880591; -.
DR KEGG; pae:PA3673; -.
DR PATRIC; fig|208964.12.peg.3842; -.
DR PseudoCAP; PA3673; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR InParanoid; Q9HXW7; -.
DR OMA; EVIYVPC; -.
DR PhylomeDB; Q9HXW7; -.
DR BioCyc; PAER208964:G1FZ6-3743-MON; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
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 GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
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..834
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195228"
FT MOTIF 310..315
FT /note="HXXXXD motif"
SQ SEQUENCE 834 AA; 94816 MW; C668FB7242B3681D CRC64;
MPRYPFRRFG FGALRRLLYL WVRSETINQS AFTLKIDRSK PVLYVLQQPS VSDLAVVDTE
CRKAGLPRPV MPVAVGDAIE PAAFFYLTPE PDWLGRQDKR GASPTLVRML AAVGQNGLDD
AQIIPVSVFW GQSPDSESSP WKLLFADNWA VTGRLRKLAR ILILGRKTRV QFSAPIHLRE
LVEQGKGHER TLRMVNRILR VHFRNLKTAV IGPDLSHRRN LVKGLLRAPL VRQAISEECE
SERISQEKAE GIALRYANEI ASDFSYPVIR FLEVILSWFW NKLYEGVKVN HIERVQDVAQ
GNEIVYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVIGSILRR GGAFFMRRSF
KGNQLYTAVF NEYLHTLFSR GFSTEYFVEG GRSRTGRMLH PRTGMLAITL RSFLRDSRRP
IVFVPVYIGY ERVLEGRTYL GELRGATKKK ESIFDLFKVV GALKQRFGQV WVNFGEPIHL
DQFLDRHQPD WQDQDLGPEY RPDWLPQTTN LLAKDVARHL NDAAAINPVN LVALALLSTS
RQALDESALA RILDLYLALL RKVPYSPSAT LPDGDGQALI EYVKSMNLLA EQKDALGRIL
YLDEQNAVLA TYYRNNVLHV FALPALIASF FQSNSRISRE QLLRFARALY PYLQAELFIR
WSLDELDAVI DQWLAALVEQ DLLRQENDTF IRPAPSSRQY VLLILLARSV TQTLQRFYMA
IALLLNAGQN ALTAEELENL CTVMAQRLSI LHGLNAPEFF DKSLFRHFIQ TLLDLRVLRK
DEAGKLSYHE LLGELAEGAA KRVLPAEIRL SIRQVALERP AEEAAAESND AAAN
