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Database: UniProt
Entry: R6F2L6_9FIRM
LinkDB: R6F2L6_9FIRM
Original site: R6F2L6_9FIRM 
ID   R6F2L6_9FIRM            Unreviewed;       391 AA.
AC   R6F2L6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:CDB03649.1};
GN   ORFNames=BN497_01167 {ECO:0000313|EMBL:CDB03649.1};
OS   Firmicutes bacterium CAG:145.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263005 {ECO:0000313|EMBL:CDB03649.1, ECO:0000313|Proteomes:UP000018044};
RN   [1] {ECO:0000313|EMBL:CDB03649.1, ECO:0000313|Proteomes:UP000018044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:145 {ECO:0000313|Proteomes:UP000018044};
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:CDB03649.1}.
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DR   EMBL; CBCX010000131; CDB03649.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6F2L6; -.
DR   STRING; 1263005.BN497_01167; -.
DR   Proteomes; UP000018044; 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:CDB03649.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018044};
KW   Transferase {ECO:0000313|EMBL:CDB03649.1}.
FT   DOMAIN          47..160
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   391 AA;  44263 MW;  B915DD12DE17B477 CRC64;
     MKDSKKIIKK PDGFIYFIAY HLVKPFLRIK CKASYDKSGL EGLKGPALVL CPHVSNIDFL
     LVAVALYPVR PTFVISEHFL ARPKLRRILT KMHVIPKKMF CPDIKTIMNI LRAKDSGNVT
     VLFPEGRLPA MGHSLQITDG TADLVKRMGV DVYTVTENGA YKTFPKWGKS GFRPGRIEVT
     TSKLFDAHSI SSMTSEEIES AIEKALFHDE DVLFEDVYYK CKSPALGLDG ILYKCPVCRA
     EFTMNSGSWD ITCSACGFKS ELDNYYRLHG GPFEKINDWY FWQQSEIDVT RPLESQTVLA
     AADEDGNLDR DAGSGVIRMD RGTISYEGTC FGQPFSFSEN VSDIKALPVS VGDHFDLYHK
     KKMYNFRLMP DPRTVIKWSM YMDKVTAESR Q
//
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