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Database: UniProt
Entry: M3C317_STRMB
LinkDB: M3C317_STRMB
Original site: M3C317_STRMB 
ID   M3C317_STRMB            Unreviewed;       256 AA.
AC   M3C317;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:EME98365.1};
GN   ORFNames=H340_21891 {ECO:0000313|EMBL:EME98365.1};
OS   Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME98365.1, ECO:0000313|Proteomes:UP000011740};
RN   [1] {ECO:0000313|EMBL:EME98365.1, ECO:0000313|Proteomes:UP000011740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40847 {ECO:0000313|EMBL:EME98365.1,
RC   ECO:0000313|Proteomes:UP000011740};
RX   PubMed=23558536;
RA   Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT   "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT   mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT   Transglutaminase.";
RL   Genome Announc. 1:E0014313-E0014313(2013).
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:EME98365.1}.
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DR   EMBL; AORZ01000080; EME98365.1; -; Genomic_DNA.
DR   RefSeq; WP_004949475.1; NZ_CP072827.1.
DR   AlphaFoldDB; M3C317; -.
DR   STRING; 1223523.H340_21891; -.
DR   PATRIC; fig|1223523.3.peg.4458; -.
DR   eggNOG; COG0204; Bacteria.
DR   Proteomes; UP000011740; Unassembled WGS sequence.
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:EME98365.1};
KW   Transferase {ECO:0000313|EMBL:EME98365.1}.
FT   DOMAIN          29..150
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   256 AA;  27698 MW;  508C750189958BF5 CRC64;
     MKLSIGGSLK LAFRPWVEGL ENVPAEGPAI LASNHLSFSD SFFLPAVLPR KITFIAKQEY
     FTSPGVKGKL TAAFFKGVGQ LPVDRSGARG AGEAAIKSGI EVLERGELFG IYPEGTRSPD
     GRLYRGKPGG LARVALATGA PVIPVAMIDT EKIQPPGKVV PKLMRPGIRI GKPLDFSRYH
     GMDGDRFILR SVTDEVMYEI MKLSGQEYVD IYATAAKRQI AEAAKKKAEE EKEAEKAAKA
     AGLDQPGEKR KRRGSE
//
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