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PLSB_SHELP
ID   PLSB_SHELP              Reviewed;         807 AA.
AC   A3QIU8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Shew_3530;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) 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; CP000606; ABO25396.1; -; Genomic_DNA.
DR   RefSeq; WP_011867325.1; NC_009092.1.
DR   AlphaFoldDB; A3QIU8; -.
DR   SMR; A3QIU8; -.
DR   STRING; 323850.Shew_3530; -.
DR   EnsemblBacteria; ABO25396; ABO25396; Shew_3530.
DR   KEGG; slo:Shew_3530; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001558; 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_1000049458"
FT   MOTIF           308..313
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   807 AA;  91491 MW;  DD866D7D63DCD02B CRC64;
     MSKQDSLWFK SLRWIQKKLV HTIVVPQDPF ADLNLDSDRP LVYVMKTESI SDIAALSEVT
     DRLGLPSPYQ PLDVEGEQAP RVVCVEGAKP LLGEREGNEF YLESFSRLLS AHKKHPELDI
     QLVPVSLYWG RTPGKEDDSM KAAVLERESP TWLRKCLMII FLGRHNFVQF SNAMSLRYMA
     DEHGTDKRIA QKLARVARVH FSRQRKVMTG PVLPNRQNLF HALLKSESMK KAILEEAQSK
     KISEAKARET AMEYLDEIAA DYSDSLVRIA ERFLTWLWNK LYKGINIKGA EQIRQLHHDG
     HEIVYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG GAFFIRRSFR
     GNKLYTAVFR EYLDQLFAKG YSVEYFTEGG RSRTGRLLAP KTGMIAMTLN SVLRGVERPV
     TLVPVYLGYD HVMEVATYHK ELSGKKKQKE SVWQVFGAIR KLGNFGQGYV NFGEPITLHS
     YLNEQVPEWR EELAQDPEQK PSWLTPVVNT LANRVMTRIN DAAAVSSITL TSLVLLASEQ
     NALQRSQLEK QLDLYLSLLK SVPYTGYTSV VEGDGAKLIA QGLELKKLKL DSDPLGDIIS
     IDESLAIAMT YYRNNIIHLL VIPSLIASCL TRQDECSRDE IIATVKDFYP LLQAELFMGI
     DNLETYVNQL LDQLLAEGLI DEDKHFSVKP DGLNQLLLLA GTISETMQRY AIIFNLLAAS
     PKIERSELES DSHQLAQRLG ALHGITAPEF YDKKLYGTLS VKLKELGYLA DDSHSEDVQR
     IRTRANSLLR SSVRQTIVDS VAAEHQA
 
 
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