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Database: UniProt
Entry: T0PG89_9CLOT
LinkDB: T0PG89_9CLOT
Original site: T0PG89_9CLOT 
ID   T0PG89_9CLOT            Unreviewed;       237 AA.
AC   T0PG89;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE            EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN   ORFNames=M918_03230 {ECO:0000313|EMBL:EQB89063.1};
OS   Clostridium sp. BL8.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB89063.1, ECO:0000313|Proteomes:UP000015873};
RN   [1] {ECO:0000313|EMBL:EQB89063.1, ECO:0000313|Proteomes:UP000015873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL8 {ECO:0000313|EMBL:EQB89063.1,
RC   ECO:0000313|Proteomes:UP000015873};
RX   PubMed=25076986; DOI=10.1186/1757-4749-6-30;
RA   Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R.,
RA   Shouche Y.S.;
RT   "Genome sequencing of multidrug resistant novel Clostridium sp. BL8 reveals
RT   its potential for pathogenicity.";
RL   Gut Pathog. 6:30-30(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         ECO:0000256|RuleBase:RU361267};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004728}.
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}.
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:EQB89063.1}.
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DR   EMBL; AUPA01000054; EQB89063.1; -; Genomic_DNA.
DR   RefSeq; WP_021282479.1; NZ_AUPA01000054.1.
DR   AlphaFoldDB; T0PG89; -.
DR   STRING; 1354301.M918_03230; -.
DR   PATRIC; fig|1354301.3.peg.1380; -.
DR   OrthoDB; 9803035at2; -.
DR   Proteomes; UP000015873; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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: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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015873};
KW   Transferase {ECO:0000256|RuleBase:RU361267}.
FT   DOMAIN          74..188
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   237 AA;  26749 MW;  F952DAD9C6557010 CRC64;
     MLRTIRWYVS FAVSLIGKIP QMHTVKSLEK KGELSFRNEY IHKTTSKWAM KRVKLSGAKV
     NIYGEENIPK DIPVVFIGNH QGNFDIALFM SFIDKPKGYV AKIEMKKIPI LRNWMSYMNC
     VFMDRSSIRK SAEAIVEGVN IIKKGHSLVI FPEGTRSKGE KMGEFKAGSF KLATKTKVPI
     IPVTIKGSYK LMEANGNKIK PAEVDMFIHP AVNTANLSKE EIDSLPGKVK KIIESKL
//
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