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Database: UniProt
Entry: A0A0C9PQV3_9BACT
LinkDB: A0A0C9PQV3_9BACT
Original site: A0A0C9PQV3_9BACT 
ID   A0A0C9PQV3_9BACT        Unreviewed;       240 AA.
AC   A0A0C9PQV3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:GAN34274.1};
GN   ORFNames=BROSI_A2810 {ECO:0000313|EMBL:GAN34274.1};
OS   Candidatus Brocadia sinica JPN1.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Brocadia.
OX   NCBI_TaxID=1197129 {ECO:0000313|EMBL:GAN34274.1, ECO:0000313|Proteomes:UP000032309};
RN   [1] {ECO:0000313|EMBL:GAN34274.1, ECO:0000313|Proteomes:UP000032309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPN1 {ECO:0000313|EMBL:GAN34274.1,
RC   ECO:0000313|Proteomes:UP000032309};
RA   Oshiki M., Shinyako-Hata K., Satoh H., Okabe S.;
RT   "Draft Genome Sequence of an Anaerobic Ammonium-Oxidizing Bacterium,
RT   "Candidatus Brocadia sinica".";
RL   Genome Announc. 3:e00267-15(2015).
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:GAN34274.1}.
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DR   EMBL; BAFN01000001; GAN34274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9PQV3; -.
DR   OrthoDB; 9803035at2; -.
DR   Proteomes; UP000032309; 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:GAN34274.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032309};
KW   Transferase {ECO:0000313|EMBL:GAN34274.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          69..183
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   240 AA;  27439 MW;  B43D1706AF154BED CRC64;
     MMFTIYSWVL FVSLWMLSTL TAVILSMDTK EKENVFNAIE RFFSRIAFKL LGMKVEIQGL
     ENIPRNEPVI FISNHQSMMD IKLSLAFIPV NFSFISKDTV FYVPVLGAYM TASGHIPIQR
     TEDRKAYATL LTAVNKLTEK KSLVVFPEGT RSEDGKLGIF KRGISLIVLK SGRRVVPMAI
     CGSNQFMPKR GWLSHPEKRS VRISFGKPLS FDSSRTDREY TIYVINKLQQ EVSELMGYKQ
//
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