ID A0A144N5E6_9GAMM Unreviewed; 919 AA.
AC A0A144N5E6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113};
GN ORFNames=A3K91_0174 {ECO:0000313|EMBL:AMT95810.1};
OS Psychrobacter alimentarius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=261164 {ECO:0000313|EMBL:AMT95810.1, ECO:0000313|Proteomes:UP000076104};
RN [1] {ECO:0000313|EMBL:AMT95810.1, ECO:0000313|Proteomes:UP000076104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27889 {ECO:0000313|EMBL:AMT95810.1,
RC ECO:0000313|Proteomes:UP000076104};
RA Lee J., Kim O.-S.;
RT "Genome sequencing of Psychrobacter alimentarius PAMC 27889.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014945; AMT95810.1; -; Genomic_DNA.
DR RefSeq; WP_062843594.1; NZ_CP014945.1.
DR AlphaFoldDB; A0A144N5E6; -.
DR STRING; 261164.A3K91_0174; -.
DR KEGG; pali:A3K91_0174; -.
DR PATRIC; fig|261164.3.peg.186; -.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000076104; Chromosome.
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; 2.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 2.
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:AMT95810.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AMT95810.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 378..505
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 229..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 103271 MW; E50E3D1ACB66958A CRC64;
MIPKFLKKRI FTAPTTTDSA MTTDGNPVAS TPYAKAPINQ LYRKLSGQLL DVAVKPKLLG
ELPEFDADDQ TLIFYVLQDY SRSNSILIDL QTQEHRLPPA LVGVNDAAHR IKENAAIVFL
NHPHAKDTPL SPRLSRLVSA VLQYPELKVR LVPVSILWGR APEKEDSLFK LLTADNWEDP
SITKQLFNIG VMGRDTFVQF HPPQDLRTII DTHLKDDTED SDLVDAVTTD LKDPSEQATN
SDSKQDAAAT PHYALVATAD SNRELVRNIQ QQLTIYLDKQ RASMLGPDLS DRRNLVDKLV
YSPAIKHAIE AEAEKTGTSV RDARLLAKGY ANEMVNDYSH SIVRGFYKFL TWLWTQLYDG
VEVHHFERVR EIATDYELVY VPCHRSHVDY LLLSYVIYKS GLSIPYIAAG DNLDVPVLGP
LLRGAVAFYI RRSFRGNALY TAVLREYMHT LITRNTPIEY FIEGGRSRSG RLLPPKMGML
AMTVHSQLRQ TNKPVVFIPT YIGYERIMEG GTYVGELKGK PKESESLIGL LKVGRKIERI
FGTVHLSFGK PLYLSEFMQK FDVSANSLPA DRTDTPLDDK TSAMVDNIGV KVMQHINKAA
VVTPVSLLSL VLLSAPKAAL DEESCREQIA LYQGLAQQLA YSDDTVITDM SPQQIIDYGI
KLKLIERTPH ILGDIIQIAG KQAALLSYFR NNILHVFILL SFLAALVARN GRMERSRLDS
IAEQLYPFLQ SELFLYYPAH GLADTINKKV DTLLSHGLIV ELGDGKLSVP ESNSKCYQQL
QVLATPVGQS LERYFMTLAL LAQQGSGNLT ESEVVDLCHL LGQRLSVLYA DDIPDFFDRA
LFTSFLSALT RLDYLQKDEE TGVLTFDHRI NDIAHHAKYV LTPDMMQILH QVASLDESEI
THAITEISNK KQRKFGRKR
//
