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Database: UniProt
Entry: S3X9Z5_9ACTN
LinkDB: S3X9Z5_9ACTN
Original site: S3X9Z5_9ACTN 
ID   S3X9Z5_9ACTN            Unreviewed;       260 AA.
AC   S3X9Z5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:EPH06187.1};
GN   ORFNames=HMPREF1531_00836 {ECO:0000313|EMBL:EPH06187.1};
OS   Propionibacterium sp. oral taxon 192 str. F0372.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH06187.1, ECO:0000313|Proteomes:UP000014567};
RN   [1] {ECO:0000313|EMBL:EPH06187.1, ECO:0000313|Proteomes:UP000014567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0372 {ECO:0000313|EMBL:EPH06187.1,
RC   ECO:0000313|Proteomes:UP000014567};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA   Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:EPH06187.1}.
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DR   EMBL; ATFL01000004; EPH06187.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3X9Z5; -.
DR   STRING; 1203605.HMPREF1531_00836; -.
DR   PATRIC; fig|1203605.3.peg.871; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_2_2_11; -.
DR   OrthoDB; 9808424at2; -.
DR   Proteomes; UP000014567; 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:EPH06187.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014567};
KW   Transferase {ECO:0000313|EMBL:EPH06187.1}.
FT   DOMAIN          53..170
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          240..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  28344 MW;  9D8429AF4C68EAB8 CRC64;
     MAEIGGGRRR FTSNTNAWTT SAAQQLLLKP AVWSVLDVHV HGTENLVGVQ APYIVIGNHS
     SHFDAPLIIG ALPKKLSRRL ATGAAADTFF TRRTTATAIQ LFMNGFPVNR SGTRSHRGMA
     KQLLSDDVPL FLFPEGTRSR SGGMGPFTPG VAALAISFNC PVIPSAVVGA YAAWPPKQKR
     WSPGRPEVHV NFGIPMRPRP GEIAHEFNER LRLKVIELHD SIATAYSMPT QAEMLHRAAL
     EPGMSSRPPV RRPEQGDDNQ
//
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