ID N8Y8K0_9GAMM Unreviewed; 719 AA.
AC N8Y8K0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113};
GN ORFNames=F960_02693 {ECO:0000313|EMBL:ENV32971.1};
OS Acinetobacter gerneri DSM 14967 = CIP 107464 = MTCC 9824.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120926 {ECO:0000313|EMBL:ENV32971.1, ECO:0000313|Proteomes:UP000013117};
RN [1] {ECO:0000313|EMBL:ENV32971.1, ECO:0000313|Proteomes:UP000013117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107464 {ECO:0000313|EMBL:ENV32971.1,
RC ECO:0000313|Proteomes:UP000013117};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter gerneri CIP 107464.";
RL Submitted (FEB-2013) 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};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004765}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENV32971.1}.
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DR EMBL; APPN01000071; ENV32971.1; -; Genomic_DNA.
DR RefSeq; WP_004865485.1; NZ_KB849544.1.
DR AlphaFoldDB; N8Y8K0; -.
DR STRING; 202952.GCA_000747725_03456; -.
DR GeneID; 84210006; -.
DR PATRIC; fig|1120926.3.peg.2607; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000013117; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
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 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,
KW ECO:0000313|EMBL:ENV32971.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000013117};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ENV32971.1}.
FT DOMAIN 308..435
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 719 AA; 82801 MW; 4A6CEB01D1753D13 CRC64;
MASNAYQKFY RQFTKKILDK IVSPQILGDT QDIENISKDL HASSNICYLI QDDSLSNQVL
IDSEIEKRGM KSAFAPLKLN FINEEDSFLS LNKSKKYNEQ SRYSEKLTRL IEYLQKHPDE
DVSLIPVTVL WGRAPETEDS WYKALLSDAW STPTKIKQTL NITLYGRENY IEFHQGVSLR
GLIEAATIRE PNYFPAHYVE HELNQLFDQY KEAILGPDLS DRRTVIDKLM IADAIQEAIR
TESINKKVSL LESEIRARSY LEEIVSDYSY STIRFADIVL TKLWTQLYDG VEVHNFDMVR
ELAKDYEIIY TPCHRSHIDY LLLSYVIFKR GLMVPHIAAG INLNLPVFGQ IARGAGAYFI
RRSFNGNALY TAVFKEYVHS LLSRNTPLEY FIEGGRSRTG RLLPAKKGML AMTIQSHLRG
VTKPIVFIPT YFGYEKLLEG TSYIKELGGE KKKAESIFGI LKSIRKIEKV FGIVHVNFGE
PVYLDPILKN NAAPEHLDLH DDVPESVKKT VNDVSIDILE NINKAVVINP VSLLAFVLLN
TPKQMLSERE LIQRLEQYRT LLSLNPYDER MKITPLSNPE IIQYCIKLKQ VEYVEHDGEP
WVRVCDKQEA LLKYFSNNIL HTFVLTSNMA KILLEETCIA KSDLFLKMNE NYPAIQAEFF
LKWKVEELEA VYENILNYFK AENLIQDQDN QQIMLTADDN ELGLLQSLAD VYQSPVSEK
//
