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Database: UniProt
Entry: A0A0S2K647_9GAMM
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ID   A0A0S2K647_9GAMM        Unreviewed;       827 AA.
AC   A0A0S2K647;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432, ECO:0000256|HAMAP-Rule:MF_00393};
DE            Short=GPAT {ECO:0000256|HAMAP-Rule:MF_00393};
DE            EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113, ECO:0000256|HAMAP-Rule:MF_00393};
GN   Name=plsB {ECO:0000256|HAMAP-Rule:MF_00393};
GN   ORFNames=PP2015_3161 {ECO:0000313|EMBL:ALO43640.1};
OS   Pseudoalteromonas phenolica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO43640.1, ECO:0000313|Proteomes:UP000061457};
RN   [1] {ECO:0000313|EMBL:ALO43640.1, ECO:0000313|Proteomes:UP000061457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO43640.1,
RC   ECO:0000313|Proteomes:UP000061457};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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:0000256|ARBA:ARBA00000510, ECO:0000256|HAMAP-
CC         Rule:MF_00393};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|HAMAP-Rule:MF_00393}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00393};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00393};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00393}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
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:0000256|HAMAP-Rule:MF_00393}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC       {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|HAMAP-Rule:MF_00393}.
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DR   EMBL; CP013187; ALO43640.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S2K647; -.
DR   STRING; 161398.PP2015_3161; -.
DR   KEGG; pphe:PP2015_3161; -.
DR   PATRIC; fig|161398.10.peg.3221; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000061457; Chromosome I.
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 {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_00393};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00393}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00393};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061457};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00393}.
FT   DOMAIN          322..449
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   MOTIF           327..332
FT                   /note="HXXXXD motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ   SEQUENCE   827 AA;  93314 MW;  889B6AA3CC683F77 CRC64;
     MVSPVFPWYS IANFLAGYDM NILTRSANVI AAAVNRILVR TKLLPESPVA QFELDPSLPT
     FYVTRLNSKA DLAALAAVCK QLGLPDPREQ QTLSGKQIDR FIPLSNPTPL FGDKAKPSDA
     LELGKQIFDA FSLSPEQRAQ VVPVTILWGR NPGKEKPGIG TLFSHSMTPS WLRKFFVLLF
     SGRDNLVRFS QPIELNQLMT DKSDVDELPH KLLRVARVHF KRQKLAATGP KLPSREALFS
     GLLASPSIKK AIADEAKAKG LSHEEAKLKA KELLEEIAAN YSDAMIRVGD RILTWLWNKL
     YNGIEVKYAE RVHELTNKGH EVIYVPCHRS HMDYLLLTYV IYHQGLVPPH IAAGVNLNFF
     PAGGIFRRSG AFFIRRSFAG NKLYSAIFKE YLSQLFMKGY SVKFYTEGGR SRTGRLLPPK
     TGMLAMTMQA MLRGIERPIS IVPVYIGYEY VMEINTYLKE LAGNDKKNES IFAVFKAIKN
     LKNYGRGYLN FGEPIALQQY LNEHQPDWRA HIGDDSVKPQ WLNTQVANVA QDIMTNINSA
     AALNAVNLLA TILLSRDQFA LSKPKLLKQL DFYLALQQQA KYNDQVTLPS DSAQSLLDHA
     LKLNKFDVLT DEMGEIISIR EKERTLFNYY RNNIIHLFAV PSILAQLIYQ KTEISFESAN
     KTVNALYPLF AKEWFLTTLS EDYIANILNS FEQQKLISMD NGIIKITADK QAQAQLEMLG
     NVMHLTLERY AITTTQIINS DAIKRQQLEA DCEVLAKRLG TLHGIKSPEF FDKKVLTNLI
     SGLKEQNYIS ICEQNTIHAE EAIANLQSQL TELLPASIWQ SIHEHSS
//
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