ID S9QPK3_9RHOB Unreviewed; 460 AA.
AC S9QPK3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113};
GN ORFNames=thalar_00122 {ECO:0000313|EMBL:EPX81567.1};
OS Litoreibacter arenae DSM 19593.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX81567.1, ECO:0000313|Proteomes:UP000015351};
RN [1] {ECO:0000313|Proteomes:UP000015351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX PubMed=24501650; DOI=10.4056/sigs.4258318;
RA Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT member of the Roseobacter clade isolated from sea sand.";
RL Stand. Genomic Sci. 9:117-127(2013).
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 -!- 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:EPX81567.1}.
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DR EMBL; AONI01000005; EPX81567.1; -; Genomic_DNA.
DR RefSeq; WP_021101066.1; NZ_KE557310.1.
DR AlphaFoldDB; S9QPK3; -.
DR STRING; 1123360.thalar_00122; -.
DR PATRIC; fig|1123360.3.peg.122; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_611008_0_0_5; -.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000015351; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
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 SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:EPX81567.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015351};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPX81567.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..275
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 460 AA; 51332 MW; 82B81E19F17C5138 CRC64;
MFTTVELPVW ALVLMGVLAA VTAASHLLFP SVRWFFRRRA ERVVARLNTK LARPIQPFKL
ARRHDMIQNV LYDPDVIRAV NAYADEKGIP DNVAFETAQR YAREIVPSFS ASVYFGLGTK
LARWLSRSLY RVRVVNARGN AMAAIDPEAT VVFIINHRSN MDYVLVTYLA ARDSALSYAV
GEWARVWPLR PLIKMMGGYF IRRKSLSPLY RRILARYVQL STREGVTQAV FPEGGLSRTG
ALGKPKLGLI SYIVDGFDPN ATRDVVFVPV GLNYDRVLED RVLVAAAEDK SARFRFRIVP
VFRYVGRHLW QRLTGKFHRL GFAAVAFGEP LSLKQFLAEG AAQSTEALGE ELMARVGRVV
PILPVPLVCQ LLETAGGKLA RAELETQFAQ EVARFRASGL ELCMPTEAGG VSVERAVKEA
LRMLEVRALI RVDAGQITVT DKAPEAITYY ASSLQHFDAT
//
