ID   PLSB_AERHH              Reviewed;         807 AA.
AC   A0KEQ0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=AHA_0182;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK36673.1; -; Genomic_DNA.
DR   RefSeq; WP_011704200.1; NC_008570.1.
DR   RefSeq; YP_854715.1; NC_008570.1.
DR   AlphaFoldDB; A0KEQ0; -.
DR   SMR; A0KEQ0; -.
DR   STRING; 380703.AHA_0182; -.
DR   EnsemblBacteria; ABK36673; ABK36673; AHA_0182.
DR   KEGG; aha:AHA_0182; -.
DR   PATRIC; fig|380703.7.peg.173; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000756; 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_1000049427"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   807 AA;  91472 MW;  030E2B3C2CCC210E CRC64;
     MSLGQNISRA ILQWPVSGLV NHKSLPENPI TELKLDPARP IVYALKTSSI TDLMTLQQCC
     EDLGLPGPFT PLELNGQLLP RYVCLDRPPP LFGKRSKPLP FLQEFHQLLD LHKQDPALDI
     QVVPVTLFWG RAPGREGEEA SGWNIISSLA PNRLKKALIV ILKGRENLVR FSPPLSLRHM
     ADKHGTDEAI AHKLARVART HFSRQQLAAT GPKLPNRNLL FKQLLDSNVI QQAIEEEAQR
     EGISLEKAQK RAHGYMDEIA SDFSYRLIRL GESFLGWLWN KLYRGLSVNG AEKVRQLAQE
     GHEIVYVPCH RSHMDYLLLS YVIYHQGMVP PHIAAGINLN FWPAGPIFRH GGAFFIRRTF
     KGNPLYSTVF REYLNLLFAK GYSVEFFTEG GRSRTGRLLP PKTGMLAMTL QAMMRGLDRP
     VTLVPVYLGY EHVMEVNTYH NELKGSRKEK ESFLQVLGIL RKLRNYGRGF VNFGEPLTLN
     NYLNEHVPSW KEHIGEEERP EWMAPTVNQL AELLMTRING AAAVNGLTLS ALALLAAERH
     ALTRDELQAQ LNTYLDLLKQ VPYSPHSTIP DEDAKTLLDQ AMELNKFEVS EDKLGQIVSL
     DRYQAILLTY YRNNILHLFA MPSLVAALIE RCEGISRSEI VARCIDIYPL LKTELFLRYE
     EDELPELVDA LLAELQRQQL IEARDGGFWV NPVNQTRLLL LAESIQETLQ RYAIVLTRVL
     AQPRIEAEQL EADGLMMAER LGTLHGINAP EFFDQKLFST LIHTLRSEGY LDPGCKPDLG
     RFQALADNIV PLLSTKIRRT IQAGNRL