ID L2F9K2_9GAMM Unreviewed; 876 AA.
AC L2F9K2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113};
GN ORFNames=MOMA_02010 {ECO:0000313|EMBL:ELA09143.1};
OS Moraxella macacae 0408225.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=1230338 {ECO:0000313|EMBL:ELA09143.1, ECO:0000313|Proteomes:UP000023795};
RN [1] {ECO:0000313|EMBL:ELA09143.1, ECO:0000313|Proteomes:UP000023795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0408225 {ECO:0000313|EMBL:ELA09143.1,
RC ECO:0000313|Proteomes:UP000023795};
RX PubMed=23409273;
RA Ladner J.T., Whitehouse C.A., Koroleva G.I., Palacios G.F.;
RT "Genome Sequence of Moraxella macacae 0408225, a Novel Bacterial Species
RT Isolated from a Cynomolgus Macaque with Epistaxis.";
RL Genome Announc. 1:E00188-12(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 -!- 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:ELA09143.1}.
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DR EMBL; ANIN01000001; ELA09143.1; -; Genomic_DNA.
DR RefSeq; WP_009766963.1; NZ_ANIN01000001.1.
DR AlphaFoldDB; L2F9K2; -.
DR STRING; 1230338.MOMA_02010; -.
DR PATRIC; fig|1230338.3.peg.444; -.
DR eggNOG; COG2937; Bacteria.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000023795; 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:ELA09143.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000023795};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELA09143.1}.
FT DOMAIN 333..460
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 876 AA; 100045 MW; BB493204F5B18E0F CRC64;
MTHKTTPFQL NNLYRKLSGG LLGMAVKSQL IGKIPPLKNP TTNNHETATP LTFYVLKEYS
RSNSVLIDLE TAQHQLPEAL APVKRLEFGI DEHSAMIFIH HPKSERKDGK TVYSPRLLRL
IEAIKNHPTL NIQFVPVTIL WGRAPEKEDS LFNLFTADEW QNPSIAKQLF NIGVKGRDTY
VQFHPPKNLR DILHAESKAQ SADSNKNTAL IDNHSALQLL AQRVQNRLLG YLDKQQETIL
GPDLSDRRNE VDKILNTPAI RHAIQLDSEE HNRNIHDSKK LARRYLNEIT SDYSYAMVRF
FDRFLTWLWT QLYDGVKVQH FERVREAASD HAIVYVPCHR SHIDYLLLSY VIFKRGLRVP
YVAAGENLNI PILGQMLRNG GAFFMRRSFK GNALYNAVFR EYVHSMLLRN TPIEYFVEGG
RSRSGRLLPP KKGMLAMTVQ SHLRQSSKPI AFIPTYIGYE RIIEGSTYVD ELKGKPKESE
SLFGLLKTGK KLERIFGTVH VSFGKPLYLK DFMQKYAVLP NSLPSDRSDT PIPPNVSQMV
DNIGVKIMQR INRSAVINPV TLLSMVLLDT PHGALDEQSC LEQLALYQRL AKTLPYDEDI
TVTDARPQAI IAYSTQLKLI EKTPHVLGDL IRIANGQAPL LSYFRNNILH VYILFSLCAN
LVKHNGHITF ANVEQVASTI YPFLQAELFL QYPARTLQET LTQHIEVLIA ENIIVDKGVN
AKGERQLTTP DPNTHNYQQL TVLANAVSHS LERYFMVLAL LSQQGSNKLT KEQVVDLGHL
LGQRLSVIYE DDMPDFFDRA LFSSFLETLE RLEYIQPTEN GIIQFDNRID IMAKNADFIL
DLDVLHILHQ MARLDESEIQ RTLHQLQAKK SKRKNK
//
