ID PLSB_PASMU Reviewed; 809 AA.
AC Q9CLN7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Glycerol-3-phosphate acyltransferase;
DE Short=GPAT;
DE EC=2.3.1.15;
GN Name=plsB; OrderedLocusNames=PM1182;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03266.1; -; Genomic_DNA.
DR RefSeq; WP_005751873.1; NC_002663.1.
DR AlphaFoldDB; Q9CLN7; -.
DR SMR; Q9CLN7; -.
DR STRING; 272843.PM1182; -.
DR EnsemblBacteria; AAK03266; AAK03266; PM1182.
DR KEGG; pmu:PM1182; -.
DR PATRIC; fig|272843.6.peg.1193; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000000809; 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; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR03703; plsB; 1.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 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 SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 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..809
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195226"
FT MOTIF 306..311
FT /note="HXXXXD motif"
SQ SEQUENCE 809 AA; 92674 MW; 63CFE636A090382D CRC64;
MFSLLNMYRK VLELPLSFLV KNNPIPHHPI EELKLDPTQP MVYVLPYTSQ TDLVIFRKNC
LSVGLPDPLE KNEIEGKSLP RFVFLDEGRR FFKSKGAKEE TIQVFNQYLE LHHQRSDLDV
QIIPVSVLWG RSPGHEKQSG LPQLRLLSGL QKFIAAVWFG RDTFVRFSQA VSLRYMVNEH
GSDQAISHKL ARVAKIHFSK QRISATGPRL PNREAMFNKL LASPTILDAI QDEAKAKNIS
EEKATQEAKK ILDEIAANVN YEGLRVADRF LRWLWNKLYQ GIDVQNADRV RKLALDGHEI
VYVPCHRSHI DYLLLSYVLY HQGLVPPHIA AGINLNFWPV GGMFRRGGAF FIRRTFKGNR
LYSTIFREYL AELFHRGYSV EYFIEGGRSR TGRLLAPKTG MMSMTLQALL QGQTRPISVV
PVYVGYEHVL EVDTYAKELR GAAKEKENAG LVLRVIKKLR NLGKGYVNFG EPITLSNYLN
QHYPEWKENT QAEERAKWFN QAVDSISHQV MVNINKAAAV NAMNLTGTAL LSSRQRALSR
EQLLEQLESY QQFLQNVPYS QDIVVPTESP EKMLEHILQL ERVGIIVEKD NFGEIVRLER
NSAVLMTYYR NNIQHLFVLP SLVASIVLHY EAIQKPLVLE AVSKIYPFLK SELFLSFSYE
ELQDRVNHII TEFERQEVIK CNANMLSINK PRVRMLQLWS SGVREILQRY YITVSILEKD
PATPRASLEK DSQSVAQRLS VLHGINAPEF FDKAVFSAFI ASLKQEGYFN EEGIANTEKL
NEITEILNQV ISTEVCLTIK GAIAKIEEE
//
