ID A0A377R424_9NEIS Unreviewed; 259 AA.
AC A0A377R424;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00016139, ECO:0000256|RuleBase:RU361267};
DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN Name=plsC_3 {ECO:0000313|EMBL:STR03029.1};
GN ORFNames=NCTC13336_01921 {ECO:0000313|EMBL:STR03029.1};
OS Kingella potus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=265175 {ECO:0000313|EMBL:STR03029.1, ECO:0000313|Proteomes:UP000254293};
RN [1] {ECO:0000313|EMBL:STR03029.1, ECO:0000313|Proteomes:UP000254293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13336 {ECO:0000313|EMBL:STR03029.1,
RC ECO:0000313|Proteomes:UP000254293};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361267};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC ECO:0000256|RuleBase:RU361267}.
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DR EMBL; UGJJ01000002; STR03029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377R424; -.
DR OrthoDB; 9806880at2; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000254293; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF65; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW ECO:0000313|EMBL:STR03029.1};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Reference proteome {ECO:0000313|Proteomes:UP000254293};
KW Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:STR03029.1}.
FT DOMAIN 72..184
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 259 AA; 28391 MW; 85F81E0609A9B51F CRC64;
MSLRPTTFPT RFARLSAMLR WLFATVRRIG RLDDASQEVR NAEFAAICRD ALDILNVRLD
VRNRPSESPR GVLVVSNHVS LLDIFAITAV CPSGFVAMKE LERWPLVGRA ARNAGAVFID
RGSRKDVGLI NGAVIRSLES GQNVCFFPEA RTSCGDGILP FKAALFQSAL DARVPVQPLA
LRYFDGLNRR TEQPSFSGVN LLVSMWRIVS MREVRVRVDF LPPFAPEGDR FALKDRVEAA
VGAAVGGFAD GGGLTEEGL
//
