PLSB_VIBVY
ID PLSB_VIBVY Reviewed; 809 AA.
AC Q7MQ86;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=VV0122;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC92886.1; -; Genomic_DNA.
DR RefSeq; WP_011149131.1; NC_005139.1.
DR AlphaFoldDB; Q7MQ86; -.
DR SMR; Q7MQ86; -.
DR STRING; 672.VV93_v1c01100; -.
DR EnsemblBacteria; BAC92886; BAC92886; BAC92886.
DR KEGG; vvy:VV0122; -.
DR PATRIC; fig|196600.6.peg.170; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000002675; 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; 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..809
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195238"
FT MOTIF 306..311
FT /note="HXXXXD motif"
SQ SEQUENCE 809 AA; 90541 MW; 80C81BF8BF45201A CRC64;
MSSGQSFSHS LLKLPLSALV KGTAIPSNPI DDHHIDINKP IVYALPFRSA VDLLTLQKHA
LELGLPDPLS PLEIHGKSLK RYVFIASRPT LVQSDNDVPS DSIALFSDLL ALHAEDSELD
VQVIPATVLW GRKPGKEGNN KPYLQAMNGL QKAKAVITAG RDCLVRFSPV VSLRYMAQSH
GTDSSIAHKL ARVARIHFSR QKLAASGPDL PSRQVLFARL MKSPAIEQAI EEEAKSKNIS
MEKARKEAQD IMDEIAADFS YSLVKQGDRL LGWLWNKLYQ GLNINNAATV RRLAQDGHEI
VYVPCHRSHM DYLLLSYVLY HEGMVPPHIA AGINLNFFPA GPIFRRGGAF FIRRSFKGNR
LYSTIFREYL AELFAKGYSV EYFSEGGRSR TGRLLPAKTG MLAMTIQAML RGLNRPVTLV
PVYIGYEHVM EVATYAKELR GKRKEKENAG LVLRTLRKLR NFGLGYVNFG EPIPLNQYLN
EHAPEWTKDI DPMGASRPQW INPVVNQLAN KMMTHINDAA AANALTLCAT ALLASRQRAL
SKDSLIHQIE CYLQLLKNVP YSKTYTVPSE SAEALVEHAI SLDKFVIETD TMGDIISLDR
NQSILMTYYR NNIIHLFALP SLIAQMIIRQ ENLTVSQIQQ QVAEIYPFLK AELFLSHKEE
ELDELVVKVL NELVSQDLIS LKADKVAKNQ ANTLTLVLLG RTISETLQRY SIAFNLLVSN
PELAKADLEQ KSQDIAQRLT RLHGINAPEY FDKGVFASLF STLKQQGYLD SDGNCDSEKT
AQFATLLYAL LYPEVKLTIE ESVFQLKSA
