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Database: UniProt
Entry: R6N2T5_9FIRM
LinkDB: R6N2T5_9FIRM
Original site: R6N2T5_9FIRM 
ID   R6N2T5_9FIRM            Unreviewed;       205 AA.
AC   R6N2T5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:CDC02544.1};
GN   ORFNames=BN531_01693 {ECO:0000313|EMBL:CDC02544.1};
OS   Eubacterium sp. CAG:202.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262884 {ECO:0000313|EMBL:CDC02544.1, ECO:0000313|Proteomes:UP000017996};
RN   [1] {ECO:0000313|EMBL:CDC02544.1, ECO:0000313|Proteomes:UP000017996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:202 {ECO:0000313|Proteomes:UP000017996};
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:CDC02544.1}.
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DR   EMBL; CBEO010000116; CDC02544.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6N2T5; -.
DR   STRING; 1262884.BN531_01693; -.
DR   Proteomes; UP000017996; 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:CDC02544.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017996};
KW   Transferase {ECO:0000313|EMBL:CDC02544.1}.
FT   DOMAIN          39..151
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   205 AA;  23127 MW;  E8C7DDFE5A90974F CRC64;
     MGQSKVLYRV GQAVCRPIMK VFYRYKFINN NSIPHEGAYI IASNHMSFSD PVLLGLGQRR
     RLFFMAKQEL FKNKFFAGLI RALGAFPVER GAGDGKAIKT GEDLIKEGNV MTIFIEGGRT
     KTGEFMRPRS GCALVAQQMQ VPVIPACITI TGNPKYRFAK RVIHFGDPLT PQQLGLTPDG
     DRRQLKNATN MIMDEIKKMR EQDRK
//
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