ID A0A0C1K368_9BACT Unreviewed; 213 AA.
AC A0A0C1K368;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:KIC77176.1};
DE EC=2.3.1.51 {ECO:0000313|EMBL:KIC77176.1};
GN Name=plsC {ECO:0000313|EMBL:KIC77176.1};
GN ORFNames=DB41_CV00140 {ECO:0000313|EMBL:KIC77176.1};
OS Neochlamydia sp. TUME1.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Neochlamydia.
OX NCBI_TaxID=1478174 {ECO:0000313|EMBL:KIC77176.1, ECO:0000313|Proteomes:UP000031320};
RN [1] {ECO:0000313|EMBL:KIC77176.1, ECO:0000313|Proteomes:UP000031320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUME1 {ECO:0000313|EMBL:KIC77176.1,
RC ECO:0000313|Proteomes:UP000031320};
RX PubMed=25069652; DOI=10.1093/molbev/msu227;
RA Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA Rattei T., Subtil A., Horn M.;
RT "Massive expansion of Ubiquitination-related gene families within the
RT Chlamydiae.";
RL Mol. Biol. Evol. 31:2890-2904(2014).
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 -!- 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:KIC77176.1}.
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DR EMBL; JRXI01000012; KIC77176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1K368; -.
DR Proteomes; UP000031320; Unassembled WGS sequence.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
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:KIC77176.1};
KW Transferase {ECO:0000313|EMBL:KIC77176.1}.
FT DOMAIN 35..147
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 213 AA; 24200 MW; 1A19ED0DBDA36C02 CRC64;
MKFFYRSIYI CTKKFFSLLF RHQVYGKHHL PAGPCILAPN HASFLDPPLV AISCDEEVNF
LARGSLFNNT IFKKLISHLN SYPVGGISQD ITSLKLILQL LKDSKKVVIF PEGKRTPTGH
LLPIKPGIGM LISKSQCPII PVYIHGTYEA WPKKKWIPRL EGQTACIFGK PIYWEAYKDL
PKKKAQEEIS NAIQKSLKML NFWYLNGAQG EPP
//
