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Database: UniProt
Entry: F0SUW0_SYNGF
LinkDB: F0SUW0_SYNGF
Original site: F0SUW0_SYNGF 
ID   F0SUW0_SYNGF            Unreviewed;       237 AA.
AC   F0SUW0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   OrderedLocusNames=Sgly_2389 {ECO:0000313|EMBL:ADY56676.1};
OS   Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Syntrophobotulus.
OX   NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY56676.1, ECO:0000313|Proteomes:UP000007488};
RN   [1] {ECO:0000313|EMBL:ADY56676.1, ECO:0000313|Proteomes:UP000007488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RX   PubMed=21886864;
RA   Han C., Mwirichia R., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA   Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA   Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Brambilla E.M., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Syntrophobotulus glycolicus type strain
RT   (FlGlyR).";
RL   Stand. Genomic Sci. 4:371-380(2011).
RN   [2] {ECO:0000313|Proteomes:UP000007488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL   Submitted (FEB-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   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004728}.
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; CP002547; ADY56676.1; -; Genomic_DNA.
DR   RefSeq; WP_013625541.1; NC_015172.1.
DR   AlphaFoldDB; F0SUW0; -.
DR   STRING; 645991.Sgly_2389; -.
DR   KEGG; sgy:Sgly_2389; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_6_1_9; -.
DR   OMA; KKSLVWI; -.
DR   OrthoDB; 9803035at2; -.
DR   Proteomes; UP000007488; 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: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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:ADY56676.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000007488};
KW   Transferase {ECO:0000256|RuleBase:RU361267}.
FT   DOMAIN          74..188
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   237 AA;  26997 MW;  9636A5341DF04062 CRC64;
     MLRTFFWFIY FWLYLISVLP AQFKIERLAK ENNTASHDQL VDRTVKRWAQ SLVSLSGSKI
     KVTGEENVPA ERPVVFVSNH QGNFDIPILL GYIQKPKAFI AKVELAKMPM VSTWMRHMKC
     VFMDRSDIRQ SLRTIAEAAS YLQNGYSMVI FPEGTRSKGM ALGEFKPGSF KLAVKAKALI
     VPVTIRGSYQ IMEAQKFIIK PAEVEIVISK PIETKNLTKE QEALLPEQVR SIIQSNL
//
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