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Database: UniProt
Entry: A0A239GXS1_9FIRM
LinkDB: A0A239GXS1_9FIRM
Original site: A0A239GXS1_9FIRM 
ID   A0A239GXS1_9FIRM        Unreviewed;       239 AA.
AC   A0A239GXS1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=SAMN05446037_101925 {ECO:0000313|EMBL:SNS73950.1};
OS   Anaerovirgula multivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Anaerovirgula.
OX   NCBI_TaxID=312168 {ECO:0000313|EMBL:SNS73950.1, ECO:0000313|Proteomes:UP000198304};
RN   [1] {ECO:0000313|EMBL:SNS73950.1, ECO:0000313|Proteomes:UP000198304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCA {ECO:0000313|EMBL:SNS73950.1,
RC   ECO:0000313|Proteomes:UP000198304};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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|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}.
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DR   EMBL; FZOJ01000019; SNS73950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239GXS1; -.
DR   Proteomes; UP000198304; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   ECO:0000313|EMBL:SNS73950.1};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198304};
KW   Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:SNS73950.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..187
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   239 AA;  27350 MW;  C14BE94FF8DD8A93 CRC64;
     MRTLIWMIYF WLYAIASIIY YPKINYYVKK GLIQERREFA HKFTANWARS LIALSGSKIE
     VTGIENIPSE GAVLFASNHQ GNFDIPILMG YLQRPIGFIA KIELKKMPII SRWMKVIDCV
     FIDRKDIRQS LRVMTQAIDI LKSGQSMVIF PEGSRSMGNE MTPFKPGSLK IAARSNTPII
     PITIIGSYKM MESNNNRIQP AHVKVIISPA INPYQTEKTS DLTVTIHNII KENLIKYTH
//
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