PLSB_SHEDO
ID PLSB_SHEDO Reviewed; 807 AA.
AC Q12ID7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Sden_3514;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) 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; CP000302; ABE56789.1; -; Genomic_DNA.
DR RefSeq; WP_011497929.1; NC_007954.1.
DR AlphaFoldDB; Q12ID7; -.
DR SMR; Q12ID7; -.
DR STRING; 318161.Sden_3514; -.
DR EnsemblBacteria; ABE56789; ABE56789; Sden_3514.
DR KEGG; sdn:Sden_3514; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000001982; 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..807
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000049456"
FT MOTIF 308..313
FT /note="HXXXXD motif"
SQ SEQUENCE 807 AA; 91643 MW; C582FD38ECB0542C CRC64;
MSNYDSIFIK SLRWIQKWLV QTIVVPHDPL TDLNLDPSKP VVYVMKTESI SDLAALSGIT
ANFGLPSPYD PLTLDKVSIA RVVCLEGRKP MIGQREGGEK FLDSFTQLLA LHKQDKQLDI
QLVPVSLYWG RTPGKEDDTM KAAVFERENP TWLRKFFMIL FLGRHNFVQF SNAVSLRHMA
DEHGTDKSIA HKLVRVARVH FRRQRKVMTG PLLPNRQALF NALLKSESIK KAIEEEATNK
KISIEKARET AIVYLDEIAA DYSDSLVRIT ERFLTWLWNK LYSGINIERA EQVRQLHHDG
HEIVYVPCHR SHMDYLLISY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG GAFFIRRSFN
GNKLYTAVFR EYLDQLFAKG YSVEYFTEGG RSRTGRLLAP KTGMIAMTMN SVLRGIERPV
TLVPVYLGYD HVMEVATYHK ELSGKKKQKE SLWQVFGAIR KLGNFGQGYV NFGEPINMQN
FLTEQAPEWR AELAKDPEQK PSWFTPAVNV LANRVMTNIN GAAAASSVTL TSLILLASEQ
NALERTQLER QLDLYLNLLK KVPYTPFTSV AQGDSQQVVD HCLGLNKFIS TRDALGEIIS
IDPKIAVTMS YYRNNIIHLM VVPSLIASCL VQYEVRSRSE IKAIVNDFYP LLKAELFMGI
ADLDSYIDDI IDLLIEEQLV EESAGLSIVE SHISQLWLMA QTVSETLQRY AIIFNLLAHK
PNVERADLEN DSHLLAQRLG ALHGITAPEF YDKKLYNTLS VKLKELGYLS AVEKQVDVAR
IRDHANGLLW SSVRQTIIDS VAAEHGH
