ID A0A1Y3TKD4_9FIRM Unreviewed; 236 AA.
AC A0A1Y3TKD4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 05-DEC-2018, entry version 5.
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 ORFNames=B5G27_07750 {ECO:0000313|EMBL:OUN34619.1};
OS Lachnoclostridium sp. An76.
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX NCBI_TaxID=1965654 {ECO:0000313|EMBL:OUN34619.1, ECO:0000313|Proteomes:UP000199802};
RN [1] {ECO:0000313|EMBL:OUN34619.1, ECO:0000313|Proteomes:UP000199802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|EMBL:OUN34619.1,
RC ECO:0000313|Proteomes:UP000199802};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T.,
RA Cizek A., Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-
CC diacyl-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
CC and may constitute the binding site for the phosphate moiety of
CC the glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|RuleBase:RU361267}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:OUN34619.1}.
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DR EMBL; NFHL01000003; OUN34619.1; -; Genomic_DNA.
DR Proteomes; UP000199802; Unassembled WGS sequence.
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 InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW ECO:0000313|EMBL:OUN34619.1};
KW Complete proteome {ECO:0000313|Proteomes:UP000199802};
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:UP000199802};
KW Transferase {ECO:0000256|RuleBase:RU361267,
KW ECO:0000313|EMBL:OUN34619.1}.
FT DOMAIN 70 185 PlsC. {ECO:0000259|SMART:SM00563}.
SQ SEQUENCE 236 AA; 27261 MW; 8D400ADCBA420363 CRC64;
MKRILMMVLR NLYMVPYGWI RLCYRAAHVD KYTEEDMYAF LRWIDLHANR GGRVHIDVHG
RENIPDRDGF MFFPNHQGLY DVLAIIEASP RPFSVVAKKE IAKIPFLKQI FACMKAFMLD
REDVRQAMQV IINVTKEVQK GRNYLIFAEG TRSKNGNRVG SFKGGSFKAA TKARCPIVPV
ALIDSFKPFD TNTIRPVTVQ VHFLKPLEYE EYKDMKTTEI AALVEKRIQS VIDANI
//
