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Database: UniProt
Entry: I0GSB0_SELRL
LinkDB: I0GSB0_SELRL
Original site: I0GSB0_SELRL 
ID   I0GSB0_SELRL            Unreviewed;       199 AA.
AC   I0GSB0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE            EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN   Name=plsC {ECO:0000313|EMBL:BAL83647.1};
GN   OrderedLocusNames=SELR_19390 {ECO:0000313|EMBL:BAL83647.1};
OS   Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL83647.1, ECO:0000313|Proteomes:UP000007887};
RN   [1] {ECO:0000313|EMBL:BAL83647.1, ECO:0000313|Proteomes:UP000007887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA   Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA   Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT   TAM6421.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361267};
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       may constitute the binding site for the phosphate moiety of the
CC       glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC       ECO:0000256|RuleBase:RU361267}.
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DR   EMBL; AP012292; BAL83647.1; -; Genomic_DNA.
DR   RefSeq; WP_014425078.1; NC_017068.1.
DR   AlphaFoldDB; I0GSB0; -.
DR   KEGG; sri:SELR_19390; -.
DR   PATRIC; fig|927704.6.peg.2013; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_4_5_9; -.
DR   OMA; RPWVEGL; -.
DR   OrthoDB; 9803035at2; -.
DR   Proteomes; UP000007887; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR   PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10434:SF57; 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:BAL83647.1};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:BAL83647.1}.
FT   DOMAIN          34..146
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   199 AA;  21776 MW;  F7AF53828623C349 CRC64;
     MLYSLLQLIF GLFFKLFFRA EIYGRENMPK DGAVILAANH MSNWDPPLVA TFLHRPVSYM
     AKIELFKNPI FGRAITACHA FPVKRGAADR GAIKAAMQVL KEGRCLGLFP EGTRSRTGKL
     GKAEAGVGLI AAMSKAPIVP AAIIGTDKIF ANGGHFPKLK VIYGEPMKFE GDHKDKEALA
     AFSQSIMDKI AAMKAEYQD
//
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