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Database: UniProt
Entry: R5MEA4_9MOLU
LinkDB: R5MEA4_9MOLU
Original site: R5MEA4_9MOLU 
ID   R5MEA4_9MOLU            Unreviewed;       287 AA.
AC   R5MEA4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=BN817_00270 {ECO:0000313|EMBL:CCY87979.1};
OS   Mycoplasma sp. CAG:956.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1262908 {ECO:0000313|EMBL:CCY87979.1, ECO:0000313|Proteomes:UP000018117};
RN   [1] {ECO:0000313|EMBL:CCY87979.1, ECO:0000313|Proteomes:UP000018117}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:956 {ECO:0000313|Proteomes:UP000018117};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCY87979.1}.
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DR   EMBL; CAZA010000010; CCY87979.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5MEA4; -.
DR   STRING; 1262908.BN817_00270; -.
DR   Proteomes; UP000018117; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000018117}.
FT   DOMAIN          95..212
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   287 AA;  33097 MW;  AE4F05BCC739D9F8 CRC64;
     MIIGGSKKDV IKNIEQNVLD NELNKKVEVN DAILSDEEIT KLLDTFYKNK GKKIRYGIKH
     AIANMTVSKY MKMLDKDIVI NGAEKLKNVD LSKGAIITSN HFNPLDTFII RKLVEKVLKK
     DLYIVIQDTN LAMPGSLGFL MNYLNVIPVS KSPTYLAGTF KENLRKILNA GNIVLIYPEE
     EMWFNYRKIR PLKRGAYQYA AILNVPVISC FTKIIDTDIV DNEEFNKTTY ELNVLGVLYP
     DKDVSPRVNS INMLNEDYEW KKQAYENVYH KKLEYTFSAD DIAGYRW
//
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