ID A0A2M8S2Q1_9PAST Unreviewed; 254 AA.
AC A0A2M8S2Q1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:PJG85412.1};
GN ORFNames=CVP05_06715 {ECO:0000313|EMBL:PJG85412.1};
OS Conservatibacter flavescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Conservatibacter.
OX NCBI_TaxID=28161 {ECO:0000313|EMBL:PJG85412.1, ECO:0000313|Proteomes:UP000229329};
RN [1] {ECO:0000313|EMBL:PJG85412.1, ECO:0000313|Proteomes:UP000229329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_4 {ECO:0000313|EMBL:PJG85412.1,
RC ECO:0000313|Proteomes:UP000229329};
RA Christensen H.;
RT "Reclassification of Bisgaard taxon 7 as Conservatibacter flavescens gen.
RT nov., sp. nov.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:PJG85412.1}.
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DR EMBL; PHHA01000014; PJG85412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8S2Q1; -.
DR OrthoDB; 9812274at2; -.
DR Proteomes; UP000229329; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:PJG85412.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000229329};
KW Transferase {ECO:0000313|EMBL:PJG85412.1};
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 TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..193
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 254 AA; 28934 MW; 859E4C53CF534A31 CRC64;
MAEKLDWLRR FFGTMFGFVL FGVLGMSYKL VLAPYVKRVK KGDFSHLLQA RQSVGKIWAF
FIKYLIWVGV LEVEYRGFER LGRKGQLVVA NHPSLLDVVL ILSKESRLNC IVKKELLNNP
VMTDPIIACG FLPNTESEEM LAKSHQILQD EALLLFPEGT RTGWDGVVNL HRGAVSIGLR
SAEVITPIII KMSPPNFKKG QPWYKIPPQK IRYELIVAED IDPKALLAEK PLPIASRRLK
KQLEDLFNSH THVM
//
